Chemical components of cells Flashcards
What are the types of bonds found in important biomolecules?
Covalent bonds:
-Polar
-Non-polar
-Characterized by bond angles and lengths
-Can involve more than one electron pair (double bonds are shorter and stronger)
Noncovalent bonds:
-Ionic bonds
-Hydrogen bonds
-Hydrophobic interactions
-van der Waals forces
Which electrons determine how atoms interact?
The outermost electrons (valence electrons)
-form covalent chemical bonds between atoms by sharing valence electrons
Describe polarity and electronegativity
-Polarity of a covalent bond depends on the relative electronegativities of the participating atoms
-Electronegativity: tendency to attract electrons
What is bond strength and thermal energy
Describe ionic bonds/electrostatic interactions
-Weak attraction between oppositely charged (or opposite polarity) groups in large biomolecules are important
-Ionic bonds may be disrupted in water but deep within core of protein may still be intact
-electrostatic interactions can be attractions OR repulsions
Describe hydrogen bonds
amino acids in a polypeptide chain can be H bonded together in a folded protein
Describe hydrophobic interactions
Describe van der Waals forces
Describe the properties of water
What are acids, bases and buffers
Describe the nature of biological molecules
What are the functional groups and their purpose?
What are macromolecules
What are the 4 tyeps of biological molecules?
What are carbohydrates and how are they classified?
What is the structure of sugars?
How are sugars linked together?
What are the nutritional polysaccharides?
What are the structural polysaccharides?
What are lipids?
What are fats and fatty acids?
Fats:
-Ampipathic meaning tails (fatty acid) are hydrophobic and head (glycerol) are hydrophilic
Fatty acids:
-Differ in length (14-20 Cs) and presence of C=C
-Different properties when incorporated into cell membranes
-Saturated: No C=C, can be packed tightly and solid at room temp
-Unsaturated: Have C=C, cannot be packed tightly and liquid at room temp
What are steroids?
What are phospholipids?
What are proteins?
Describe the properties of side chains in proteins
What are the four levels of organization in protein structure
Describe protein primary structure
How do amino acid side chains influence protein folding?
What is sickle cell anemia?
-Single amino acid change within hemoglobin molecule causing a crescent or sickle-shaped red blood cell
-Glutamic acid to valine
Describe protein secondary structure
Describe protein tertiary structure
Domains:
-structural unit of tertiary structure
-Hydrophobic cores connected by loop regions
-Fold independently
-Eukaryotic proteins > or = 2 domains
-often have specific function
Describe quaternary structure
What are molecular chaperones
Explain protein misfolding and alzheimers
What are nucleic acids
Differ RNA and DNA
What are the nitrogenous bases
Differ DNA and RNA structure
Explain macromolecular assembly
