Unit 2 Biochemistry Flashcards
<p></p>
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<p>Cations</p>
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<p>= positive ions with more protons then electrons</p>
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<p>Anions</p>
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<p>= negative ions with more electrons then protons</p>
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<p>Beryllium Bohr Short form</p>
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<p>Be 2e-)2e-</p>
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<p>Sulphur Bohr short form</p>
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<p>S 2e-) 8e-) 6e-</p>
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<p>3 Main types of Intramolecular bonds:</p>
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<p>-Ionic (electron transfer)
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<br></br>-Covalent (two or more non metals share one or more pairs of electrons)
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<br></br>-Polar covalent (a covalent bond that occurs when there is an unequal sharing of electrons causing a dipole - the molecule has a positive and negative pole)</p>
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<p>Ionic Bonds</p>
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<p>= typically between metals and non metals, always a transfer of electrons from one atom to another that results in stable bonding For both atoms.</p>
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<p>Covalent bonds</p>
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<p>= when two or more NON METALS share one or more pairs of electrons. Results in a stable electron arrangement in their outer orbit.</p>
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<p>Polar Covalent Bonds</p>
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<p>= covalent bond that occurs when there is an unequal sharing of electrons. When one atom pulls stronger than the other, resulting in different polar charges at the ends of the molecule (aka DIPOLE)</p>
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<p>Dipole</p>
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<p>= molecule with one end slightly positive and the other slightly negative. The more electronegative an atom, the stronger they are at pulling the electrons to them. The higher electronegative atom will be the one slightly negative.</p>
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<p>3 Types of Intermolecular Bonds</p>
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<p>- London dispersion forces / van der Waal forces
<br></br>- Dipole-Dipole
<br></br>-Hydrogen bonding</p>
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<p>London forces</p>
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<p>= all molecules have them, very weak forces of attraction, momentary dipoles are created by the electrons in the compound that are constantly emotions. Which are constantly in motion (WEAKEST intermolecular force)</p>
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<p>Dipole-dipole forces</p>
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<p>= MEDIUM hold polar molecules together, the opposing dipoles attract</p>
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<p>Hydrogen bonding</p>
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<p>= STRONGEST formed between electropositive hydrogen dipole and an electronegative dipole of oxygen, chlorine or fluorine</p>
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<p>4 Main Types of Biochemical Reactions</p>
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<p>- hydrolysis
<br></br>-condensation
<br></br>-redox reactions
<br></br>-neutralization</p>
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<p>Hydrolysis</p>
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<p>a reaction that uses water to help break down molecules. Examples such as carbohydrate lactose into galactose glucose, or protein to amino acids (in presence of enzymes)</p>
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<p>Condensation</p>
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<p>= when two molecules combine together to form one molecule. OFTEN water is produced, which is why it’s also known as dehydration synthesis. Examples being an upstream amino meets a downstream amino acid to create protein and water.</p>
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<p>Redox Reaction</p>
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<p>an electron transfer between two substances (an oxidation and reduction process)</p>
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<p>An important redox reaction used by animals to make energy</p>
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<p>CELLULAR RESPIRATION, combines glucose and oxygen to produce carbon dioxide, water and energy (ATP)</p>
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<p>Neutralization</p>
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<p>= an ACID and a BASE reaction to produce water and a salt. Happens often in digestive system.</p>
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<p>Oxidation</p>
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<p>= process of losing electrons</p>
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<p>Reduction</p>
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<p>= process of gaining electrons</p>
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<p>what are 3 molecules that PURE water contains</p>
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<p>H2O, H+ ions, and OH- ions</p>
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<p>how our hydrogen ions and hydroxide ions produce in pure water?</p>
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<p>a natural process called ionization</p>
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<p>ionization</p>
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<p>the dissociation of a molecule into ions</p>
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<p>definition of Acids</p>
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<p>substances that when dissolved in water increase the concentration of H+ (hydrogen ions).</p>
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<p>definition of Bases</p>
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<p>substances that when dissolved in water increase the concentration of hydroxide ions (OH-)</p>
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<p>4 properties of Acids</p>
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<p>- sour taste
<br></br>-conducts electricity
<br></br>- Turns litmus paper red
<br></br>- Has a pH below 7</p>
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<p>4 properties of Bases</p>
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<p>- bitter taste
<br></br>-slippery feel
<br></br>- litmus paper turns blue
<br></br>-pH above 7</p>
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<p>why is pure water neutral</p>
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<p>it contains an equal number of hydrogen and hydroxide ions</p>
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<p>acidity of an aqueous solution is expressed in terms of wht</p>
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<p>hydrogen ion concentration in mol/L</p>
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<p>pH is measured on a logarithmic scale expressed in this formula</p>
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<p>pH = -log(10 subscript)[H+]</p>
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<p>the stronger an acid or base...</p>
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<p>the more they completely ionize when dissolve in water</p>
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<p>weak acids and bases are</p>
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<p>reversible and can proceed in both directions</p>
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<p>what is the strength of most organic acid and bases</p>
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<p>weak</p>
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<p>when an acid and base react what is produced</p>
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<p>a salt and water</p>
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<p>what is the salt produced from in a neutralization reaction</p>
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<p>the metal cations</p>
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<p>what is the water produced from in a neutralization</p>
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<p>non-metal anions</p>
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<p>acid-base buffers</p>
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<p>solutions that are able to maintain nearly constant pH levels. Despite fluctuating environmental conditions.</p>
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<p>how do acid-base buffers maintain pH levels</p>
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<p>by taking up excess hydrogen or hydroxide ions, neutralizing excess acid or base</p>
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<p>examples of acid base buffers in body</p>
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<p>-proteins (red blood cells)
<br></br>- amino acids (glycine amino acid)
<br></br>- carbonic acids</p>
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<p>optimal pH level of blood</p>
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<p>7.4</p>
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<p>what buffer operates in blood and extracellular fluid to maintain pH level</p>
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<p>carbonic acid-bicarbonate buffer</p>
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<p>how is carbonic acid bicarbonate buffer made + chemical equation (give it in molecular formula as well as identify name of each molecule)</p>
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<p>by the reaction of carbon dioxide with cater to form carbonic acid that ionizes to form bicarbonate and hydrogen
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<br></br>H2O + CO2 <-> H2CO3 <-> HCO-(3subscript) + H+</p>
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<p>polymer vs macromolecule</p>
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<p>-Polymers are mostly made up of smaller repeating units (monomers)
<br></br>- Most macromolecules are due to polymerization (becoming polymer macromolecule)
<br></br>- Some macromolecules are due to chemical bonding of more atoms
<br></br>- main difference is that polymers contain repeating units that represent the monomers whereas not all macromolecules have a monomer in their structure.
<br></br>-macromolecules are an umbrella term</p>
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<p>name this functional group, polarity, solubility, acidtiy, general structural features</p>
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<br></br><p style="text-align:center;"><span><img></img></span></p>
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<br></br><p style="text-align:center;"><span><img></img></span></p>
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<p>Hydroxyl group</p>
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<br></br><p style="text-align:center;"><span>Properties: polar, hydrophilic</span></p>
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<br></br><p style="text-align:center;">Structurally the addition of an -OH group, a hydroxyl</p>
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<br></br><p style="text-align:center;"><span><img></img></span><span><img></img></span></p>
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<p>name this functional group, polarity, solubility, acidtiy, general structural features</p>
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<p>Sulffhydryl group</p>
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<br></br><p style="text-align:center;"></p>
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<br></br><p style="text-align:center;">Polar, hydrophilic</p>
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<br></br><p style="text-align:center;">Contains an SH group, sulfur with hydrogen</p>
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<p>name this functional group, polarity, solubility, acidtiy, general structural features</p>
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<p>Carbonyl group</p>
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<br></br><p style="text-align:center;">polar, hydrophilic</p>
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<br></br><p style="text-align:center;">Has a carbon double bonded to an oxygen, but the carbon is connected to 2 different sides</p>
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<p>name this functional group, polarity, solubility, acidtiy, general structural features</p>
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<p>Carboxyl group</p>
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<br></br><p style="text-align:center;">acidci, polar, hydrophilic</p>
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<br></br><p style="text-align:center;">similar to a carbonyl group, has a carbon double bonded to an oxygen, and is connected to the R group but additional a hydroxyl (OH) group</p>
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<p>name this functional group, polarity, solubility, acidtiy, general structural features</p>
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<p>Amino group</p>
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<br></br><p style="text-align:center;">Basic, polar, hydrophilic</p>
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<br></br><p style="text-align:center;">it is a nitrogen attached to R group plus two hydrogens, characterized by the presence of nitrogen</p>
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<p>name this functional group, polarity, solubility, acidtiy, general structural features</p>
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<p>phosphate group</p>
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<br></br><p style="text-align:center;">acidic, polar, hydrophilic</p>
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<br></br><p style="text-align:center;">a phosphorus attached to four oxygens (one double bond, two hydroxyls, and oxygen attached to R group)</p>
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<p>these reactions break down</p>
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<p>catabolic</p>
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<p>these reactions build up</p>
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<p>anabolic</p>
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<p>what reaction is required to form polymers and why</p>
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<p>condensation reaction/dehydration synthesis because water must be removed to join the molecules together</p>
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<p>what are the four macromolecules of life</p>
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<p>carbohydrates
<br></br>proteins
<br></br>lipids
<br></br>nucleic acids</p>
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<p>uses for carbohydrates</p>
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<p>building materials for energy ; cell identification and communication</p>
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<p>2 groups of carbohydrates + examples of each</p>
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<p>Simple = Monosaccharides, Disaccharides, Oligosaccharides (glucose, lactose)
<br></br>Complex = Polysaccharides (Starch, Glycogen, Cellulose, Chitin)</p>
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<p>two types of monosaccharides + how they are identified</p>
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<p>aldoses and ketoses ; identified by the location of their carbonyl functional group</p>
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<p>the three aldoses and location of their carbonyl functional group</p>
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<p>Ribose, glucose, and galactose [carbonyl group on the endmost carbon-opposite of hydroxyl group]</p>
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<p>the two ketoses and location of their carbonyl group</p>
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<p>ribulose and fructose [ carbonyl group located on the second carbon, opposite end of the hydroxyl group]</p>
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<p>the most important monsaccharide used for immediate energy ; considered the energy currency of the body</p>
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<p>glucose</p>
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<p>Isomers</p>
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<p>= same chemical formula but different arrangement of atoms and different chemical properties.</p>
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<p>Glucose and Galactose have the same chemical formula but different arrangement of atoms - what kind of isomerism is this and what is their chemical formula</p>
<p></p>
<p>structural isomers ;C6H12O6</p>
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<p>which molecule is this and label which is alpha and which is beta, explain the distinction of the two</p>
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<p>glucose; the alpha glucose has the first carbon's hydroxyl group "down" or opposing the sixth carbon direction, while beta glucose hydroxyl group is "up" or same as sixth carbon direction</p>
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<p>what form do 5 carbon or more monosaccharides take in water? when dry?</p>
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<p>ring structures in water ; linear/chain structures when dry</p>
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<p>what kind of sugars are usually consumed in food</p>
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<p>disaccharides</p>
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<p>what covalent bonds are formed to join monosaccharides together</p>
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<p>glycosidic linkages</p>
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<p>what does the prefix oligo mean</p>
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<p>few</p>
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<p>how many sugars are in oligosaccharides</p>
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<p>about 3-10</p>
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<p>glucose + glucose =</p>
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<p>matltose + water</p>
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<p>glucose + fructose =</p>
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<p>sucrose + water</p>
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<p>glucose + galactose =</p>
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<p>lactose + water</p>
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<p>name the two molecules, how you know, and what products are likely to be formed, with which type of reaction</p>
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<p>twoalpha glucose, based of position of hydroxyl. two glucose form maltose and water ; and anabolic reaction andcondensation/dehydration synthesis reaction</p>
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<p>how many monosaccharides are typically in a poly saccharides</p>
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<p>several hundred to several thousands</p>
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<p>4 types of polysaccharides</p>
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<p>Starch</p>
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<br></br><p>Glycogen</p>
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<br></br><p>Cellulose</p>
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<br></br><p>Chitin</p>
<p></p>
<p>2 types of glycosidic bonds</p>
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<p>Alpha (α) +Beta (β)</p>
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<p>describeBeta (β) glycosidic bonds</p>
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<p>when the carbon-1 on the first carbohydrate and the carbon-4 on the other carbohydrate are covalently bonded and the -OH group on the Carbon-1 above the glucose ring</p>
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<p>describeAlpha (α) glycosidic bonds</p>
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<p>means that the carbon-1 on the first carbohydrate and carbon-4 on the other carbohydrate are covalently bonded and the -OH group on the Carbon-1 below the glucose ring</p>
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<p>describe amylose and what kind of carbohydrate it is</p>
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<p>starch molecule ; made up of a chain of glucose bonded in alpha 1-4 glycosidic links</p>
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<p>describe amylopectin and what kind of carbohydrate it is</p>
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<p>starch molecule ; made up of 2 by 3 branchedchain of glucose bonded in alpha 1-6 glycosidic links</p>
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<p>main energy storage for molecules</p>
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<p>glycogen</p>
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<p>what converts excess glucose into glycogen</p>
<p></p>
<p>muscles and liver</p>
<p></p>
<p>what is glycogen composed of</p>
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<p>alpha1-4 links and alapha 1-6 links for branches</p>
<p></p>
<p>composed of beta 1-4 links, not coiled or branched chains, ideal building material for plants/cell walls</p>
<p></p>
<p>cellulose</p>
<p></p>
<p>undigestiable carbohydrate ; form of fibre that aids in egestion/BM ; can be used for paper or fabrics</p>
<p></p>
<p>cellulose</p>
<p></p>
<p>describe the beta 1-4 glysodic linkages in cellulose</p>
<p></p>
<p>glucose change where the glycosidic linkages are up and down of glucose as the glucose molecules are upside down every other in relation to each other</p>
<p></p>
<p>chitin is a polymer of</p>
<p></p>
<p>N-acetylglucosamine</p>
<p></p>
<p>what is the composition ofN-acetylglucosamine</p>
<p></p>
<p>it a glucose molecule with a nitrogen group attached to the second carbon</p>
<p></p>
<p>this carbohydrate is used in surgical thread and exoskeletons due to strength</p>
<p></p>
<p>chitin</p>
<p></p>
<p>function and monomers of proteins, and 6 examples of them</p>
<p></p>
<p>- involved in almost everything cells do</p>
<br></br>
<br></br><p style="text-align:center;">- can be enzymes, immunoglobin, hemoglobin, keratin, fibrin etc.</p>
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<br></br><p style="text-align:center;">- amino acid monomers</p>
<p></p>
<p>what determines the type of protein</p>
<p></p>
<p>the number of, type, and arrangement of amino acids in the protein</p>
<p></p>
<p>how many amino acids are there</p>
<p></p>
<p>20</p>
<p></p>
<p>3 distinct parts of amino acids</p>
<p></p>
<p>- amino group (NH2)</p>
<br></br>
<br></br><p style="text-align:center;">- carboxylic acid group (COOH)</p>
<br></br>
<br></br><p style="text-align:center;">- a radical/R group/side chain that disttinguishes the amino acids from one another</p>
<p></p>
<p>how does the R group in an amino acid make them different</p>
<p></p>
<p>- it can determine if the amino acids polarity/solubility and acidity</p>
<p></p>
<p>name the 9 essential amino acids and why they are essential</p>
<p></p>
<p>histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine</p>
<br></br>
<br></br><p style="text-align:center;">essential because we cant manufacture them in our cells and must obtain from our diet</p>
<p>Final stage of a protein</p>
<p>= called conformation / folded / compact</p>
<p>What shape generally are proteins</p>
<p>- globular // rolled up into balls</p>
<p>What is conformation the result of</p>
<p>- amino acid sequence it contains and how they interact with each other (molecularly/polarity)</p>
<p>4 Stages of Protein Structure</p>
<p>Primary protein structure = sequence of a chain of amino acids
<br></br>
<br></br>Secondary Protein structure = when sequence of amino acids are linked by hydrogen bonds
<br></br>
<br></br>Tertiary protein structure = occurs when certain attractions are present between alpha helices and pleated sheets
<br></br>
<br></br>Quaternary protein structure = a proteins consisting of more than one amino acid chain</p>
<p>Polypetide chain</p>
<p>- simple chain of amino acids</p>
<p>What determines a proteins sequence of amino acids</p>
<p>Dna of a gene</p>
<p>Describe proteins in primary structure</p>
<p>- 1 degree structure ; simple chain of amino acids/polypeptide chain ; can be an combo (20 to the power of X)</p>
<p>Describe Secondayry protein structure</p>
<p>- 2 degree; polypeptide chain begans folding and coiling as it grows ; either alpha helix (tight coils of H bonds every 4th peptide bond) or a beta pleated sheets (hydrogen bonds formed between parallel stretches to form sheets)</p>
<p>Disulphide bridges</p>
<p>- covalent bonds between sulphur atoms ; most common bonds occuring in tertiary protein stage</p>
<p>Describe tertiary Protein structure</p>
<p>- 3 degree structure ; additional folding between pleated sheets and alpha helix chains ; caused by the varied radical groups ; disuphide bridges forms that help build the globular structure which can be the final structure</p>
<p>Describe the Quaternary protein stage</p>
<p>- 4 degree stage ; not all proteins have this ; sometimes 2 or more polypeptide chains join to make a functional protein ; this structure depends on how the polypeptides join together</p>
<p>Describe 5 characterstics of lipids</p>
<p>Group of organic molecules that dissolve in non-polar substances, but generally not in water (insoluble in water)
<br></br>Efficient energy storage molecules that yield about twice the amount of chemical energy per gram that carbs or proteins
<br></br>Important for physical and thermal insulation for the body, key components for cell membranes and act as raw materials for the synthesis of hormones
<br></br>Mostly made up of hydrogen, carbon and oxygen
<br></br>Some form chains other rings</p>
<p>4 Families of Lipids</p>
<p>- Fats ; Phospholipids ; Steroids ; Waxes</p>
<p>3 traits of Fats</p>
<p>- Most common for of energy storage and insulation in plants and animals
<br></br>Composed of one glycerol and a maximum of 3 fatty acid chains
<br></br>Fatty acid chain contains between 16-18 carbons and has a terminal carboxylic acid</p>
<p>Define and describe how a fat molecule is formed</p>
<p>- dehydration synthesis where hydroxyl from the glycerol combines the the H from the carboxylic acid to create ester linkage and water. This process is called esterification</p>
<p>Describe 4 traitseach of Saturated and Unsaturated Fatty Acids</p>
<p>Describe the structure of a phospholipid</p>
<p>Describe the permeability of the phospoholipid bilayer</p>
<p>Sterols</p>
<p>= subgroup of steroids which are also lipids ; compact hydrophobic molecules containing four fused hydrocarbon rings</p>
<p>defineCholesterol</p>
<p>a sterol ; important because it affects membrane’s fluidity, provided support to membrane and acts as a messenger in cell communication during development. Can also be converted to Vitamin D. Too much cholesterol can lead to clogged arteries and cardiovascular disease.</p>
<p>gametes</p>
<p>(egg and sperm cells)</p>
<p>Steroids molecules of derivatives of what molecule, and examples</p>
<p>derivatives of - choloesterol (estradiol ; testosterone ; progesterone)</p>
<p>4 traits of waxes</p>
<p></p>
<p>Hydrophobic</p>
<p>Long-chain fatty acids linked to alcohols or carbon rings</p>
<p>Waxes often form waterproof coatings such as beeswax, paraffin</p>
<p>Used to manufacture items such as fuel, candles</p>
<p>4 places where nucleic acids are found</p>
<p>DNA (deoxyriobnucleic acid)</p>
<p>RNA (ribonucleic acid)</p>
<p>ATP (adenosine triphosphate)</p>
<p>Nucleotide coenzymes (NAD+, NADP+, and FAD)</p>
<p>Monomers of nucleic acids</p>
<p>- nucleotides</p>
<p>Describe nucleotide structure</p>
<p>Consist of nitrogenous base, five carbon sugar (ribose group), and a phosphate group</p>
<p>Phosphate and ribose groups are joined together by a phosphodiester linkage.</p>
Name the 5 nucleotides ; identify which one is found only in RNA
- Thymine - Cytosine - Adenine - Guanine - Uracil (RNA only)
Distinction of purines and pyrimidines and which nucleotides are in each -
Purines = double ring structure//Adrenine+Guanine //// Pyrimidines = triple ring structure (Cytosine/Thymine/Uracil)
Why do purines and pyrmidines not bond with themselves (i,e. Purine to purine)
- because pyrimidine hydorgen positions are unfavouriable with hydroges being too far part; while purine are too closes
What test is for simple sugars/monosaccharides and what colour range does it turn (which indicates it’s present) t -
Benedict’s reagent ; light blue - red to brown – darkest means simple sugar is present
What test for complex carbs/polysaccharides/starch and what colour range does it turn (which indicates it’s present -
Iodine Test with Lugol’s Solution (light brown to deep purple/black if starch is present)
What tests for lipids and what colour range does it turn (which indicates it’s present -
Sudan IV Lipid Test
Turns from a pink to a red colour, if lipids are present
What tests for proteins and what colour range does it turn (which indicates it’s present) - Biuret’s Protein Test
Changes light blue to deep purple when proteins are present
Biuret’s Protein Test
Changes light blue to deep purple when proteins are present
Describe 5 qualities of enzymes
protein catalyst that speed up chemical reactions, without being consumed by the reactions themselves.
Composed of amino acids arranged in tertiary or quaternary structures with complex conformations (shapes)
Can be used to join together two molecules or break one molecule into two parts
Names of enzymes usually end in “ase”
Enzymes are specific to a particular substrate (reactant). For instance, maltase cannot hydrolyze the substrate sucrose.
How structure of enzymes lower the Ea
By attaching to the reactants and positioning them in optimal orientation to break or make chemical bonds between them .
define and explain enzyme substrate complex
Enzyme-Substrate Complex = structure when enzyme is attached to its substrate
One substrate attaches, the active site changes shape slightly to hold n to the substrate - this change in shape/conformation is called “induced fit”. Activity site continues to conform until substrate is completely bound.
Once substrate is optimally positioned, the reaction can proceed
Describe the 4 steps to how enzyme catalyzes a reaction
- enzyme and substrate first combine on a specific area of the enzyme called the active site, to form the enzyme substrate complex.
- enzyme substrate complex combines with water (hydrolysis), which changes the shape of the enzyme slightly so that the substrate can break apart into glucose and fructose more easily.
- reaction takes place and the sucrose molecule is broken up into the two monomers, fructose and glucose.
- the enzyme is released unchanged, ready to react again with a new substrate molecule.
For catabolic reactions enzymes decrease the Ea
by stretching and bending chemical bonds that need to break.
For anabolic reactions enzymes decrease the Ea
by forcing the molecules together in the right way to cause the bonds to form more easily
Coenzymes are
“helpers” molecules to enzymes and they help moving molecules from one enzyme to another
Many coenzymes are derived from
vitamins, such as NAD- is a derivative of vitamin B3 (niacin)
The allosteric site is a place on an enzyme:
that will not bind substrates that bind to the active site
that will bind to other specific molecules that will change the shape of the enzyme and influence its ability to be active or not.
The allosteric site is involved in turning the enzyme “on” and “off.”
two types of enzyme regulation are:
competitive (when enzyme activation/inhibition happens on an active site) and non-competitive (when enzyme activation or inhibition happens on the allosteric site)
Allosteric activators
- instigate the process of activation that makes all active sites available
Feedback inhibition
= occurs in metabolic pathways involving sequential reactions in which each step is catalyzed by specific enzyme ; regulatory method of metabolic control that cells use in which products of a reaction allosterically inhibit an enzyme that catalyzes a reaction in the same metabolic pathway ; example of a negative feedback process
Negative feedback process
= process that as amount of product produced increases, rate of reaction decreases
Factors that effect enzyme activity
temp ; pH; concentration of enzyme and substrate; surface area
Organelle’s
= specialized structures that work together to make a cell function effectively
4 traits of Cell Membrane
Separates cytoplasm from external environment
Acts like a security guard, controlling what can get in or out
Allows essential molecules into the cell and allows metabolic waste to leave
Phospholipids which make up the majority of cell membrane
Phospholipids
Has a “head” containing a phosphate group that is hydrophilic
Has a “tail” containing two fatty-acid chains that are hydrophobic
The hydrophilic head has a polar phosphate group (PO4). The tail has a glycerol molecule attached to two fatty-acid chains that are non polar.This means two of these molecules will join tail-to-tail when placed in water ; one of the fatty acids has kink/double bond/unsaturated which means helps create passageways in the membrane.
Phospholipid bilayer
Double layer of phospholipids that has an outside layer (hydrophilic heads) that face watery environment (inside and outside of the cell)
Inside layer of hydrophobic fatty acid tails which face inward
Cholesterol molecules are free to drift around within lipid bilayer in order to
fix any breaks in the membrane as well as maintain fluid condition of the bilayer ; when cold cholesterol keeps phospholipids apart; when warm cholesterol attaches to the phospholipids to stabilize the membrane.
Integral Proteins in cell membrane
= proteins embedded in membrane and function as channels through which ions and other molecules can travel in and out of the cell
Fluid-mosaic model of cell membrane
Combo of lipid bilayer, proteins, and cholesterol = fluid-mosaic model of cell membrane
Called fluid because membrane is not completely solid and can adjust itself to maintain a seal around cytoplasm
Called mosaic because membrane contains several kinds of molecules embedded in it
Glycoproteins in cell membrane
Proteins attached to carbohydrate
Act as receptor sites for hormones and aid in the cell’s adhesion to other cells
3 Processes which Molecules move in and out of the cell:
Passive transport
Active Transport
Use of vehicles to move very large molecules around
Equilibrium
= equal concentration of particles throughout the solution
Diffusion =
movement of molecules from an area of higher concentration to area of lower concentration ; many molecules (partic. Small, uncharged ones like O, CO2) move easily through cell membrane due to diffusion ; moving from high to low concentration is known as moving along the concentration gradient ;
Factors that affect how fast diffusion occurs:
State of Matter = diffuses more rapid in a gas then a liquid
Temperature = diffuses more rapid at higher temp.
Size of molecule = large molecules cannot diffuse across cell memb.
Osmosis
= diffusion of water across a selectively permeable membrane ; water moves high to low water conc // low to high solute concentration. Until equilibrium is reached. Often categorized in 3 ways: iso, hyper, and hypo tonic
Hypertonic
fluid surrounding the cell has a higher solute concentration than cytoplasm resulting in water leaving the cell
Isotonic:
equivalent solute concentration ; no net water movement occurs
Hypotonic:
solute concentration of fluid surrounding the cell is less than that of the cell’s cytoplasm, and water enter the cell
Osmosis potential of solutions can be measured with
an osmometer which is a tube with a permeable membrane at one end
osomotic potential of the test solution is measure in relation to the concentration inside the tube by:
Solution of known solute concentration is placed in the tube (osmometer)
Change in height of the fluid in the tube before and after inserting osmometer indicates osmotic potential
**If water leaves osmometer - the solution is hypotonic
If water enters osmometer - solution is hypertonic
Stays the same = isotonic solution
Facilitated diffusion =
molecules enter the cell with “helper molecules” known as transport proteins. They move materials in and out of cells along the concentration gradient (high to low) so no energy is required. Their protein structure allows them to be highly selective.
Active transport is used to
maintain intracellular environment that is different from outside of cell, such as:
- Store nutrients already in high concentration in cell
- Remove harmful waste
- Homeostasis - to maintain a constant internal environment even if external environment changes
Process of active transport of an ion that requires an input of cellular energy (ATP)
- Ion is drawn onto transport protein
- ATP is used to move the ion through the membrane
- Ion is released on other side of membrane where it’s concentration is higher
What is a vesicle
when cell membrane folds in on itself to wrap around and seal large objects in a sac
Two ways in which vesicles are used to move materials across cell membranes:
Endocytosis - bring materials into cell
Exocytosis - bring materials out of cell
Phagocytosis =
cell eating = cells engulf large solid particles = immune cells engulf bacteria
Pinocytosis =
cell drinking = liquid droplets enter the cell, along with any small particles they may contain = occurs all the time in most cells
Receptor-mediated endocytosis =
RME = enables cell to acquire bulk quantities of specific substances - uses receptor to recognie and bind molecules before they are engulfed = how molecules such as cholesterol enter the cell, too much cholesterol builds up in walls of arteries and veins where it hardens
Exocytosis -
transporting out of the cell - particularly large waste - lysomomes often break down wastes and other toxins inside of the cell and then vesicles transported out of the cell in a vesicle
