Midterm prep Flashcards
(259 cards)
4/2 He = What is the mass number and the atomic number.
4 is the mass number which is number of protons and neutrons
2 is the atomic number thats number of protons
What is an isotope?
Same number of protons different number of neutrons -> making it more unstable
What are the 6 essential elements to life (bonus points for the 3 key salt making elements)
CHOPNS (Na, Cl, Mg)
What is the electronegativity order for some of the most recurring elements in bio (H, N, O, and C)
H<C<N<O
What does hydrophilic mean?
Water-loving. Polar and ions dissolve in water.
What does hydrophobic mean?
Water fearing. Non-polar molecule do no dissolve in water.
What does hydrophobic interactions mean?
Water forces non-polar molecules together to minimize the disruption to the H-bonding in the water.
Rank the inter/intramolecular forces as seen in bio
- Covalent bonding
- Hydrogen bonding (ITS FON TO HYDROGEN BOND)
- Ionic Bonding (in the case of bio this occurs mainly inside protiens and is on the relatively weaker side)
- Hydrophobic Interactions
- Van der Waals forces (dipole-dipole, LDFs)
What are acids (provide an example of a strong and weak acid)
Acids release H+ ions in a solution. Strong acids (ei HCl) dissociate completely whereas weak acids (Carboxyl groups (-COOH) dissociates partially and reversibly.
What are bases (provide an example of a strong and weak base)
Bases accept H+s in a solution and releases OH-. A strong base (ei NaOH) ionizes completely to form to ions. A weak acid (ei amino group (-NH2) by partially and reversibly accepting H+ to form NH3.
What is a buffer?
makes the overall solution resistant to pH change as they react with both acids and bases. It is made of a weak acid and its conjugate base at a 1/2 equivilance point. They are at equimolarity!
What are the the functional groups discussed in class and which are the 3 most important?
The 3 most improtant are hydroxol (OH), Carboxyl (O-C=O), and amino (-NH2). The other groups are Carbonyl (=O-H), Phosphate (PO4), and sulfyd groups (SH)
What are macromolecules provide examples?
Macromolecules are large molecules (ei proteins. nucleic acids, lipids, and carbohydrates).
How are proteins made?
Monomers are added together via a condensation reaction (water is released) forming a polymer
How are proteins broken down?
They are broken down via hydrolysis where the monomers are split apart within the polymer using water.
Characteristics of proteins
Polymers of amino acids
proteins range in size from a few amino acids (ei peptide) to thousands (ei titan)
There are ionized and non-ionized amino acids
How many amino acids are there?
20 in life
What is protein folding determined by?
- IMFs
- Sequences of aas
What is the R group and how does it vary in ionized/non-ionized aas?
R determines the identity of the amino acid. It can be C/H for any non polar amino acids. Charged (ei NH2, or HO-C=O). Or polar (ei O)
What is the general amino acid shape and what differs.
R differs but the general structure is amino group and carboxyl group
What is a peptide bond?
A special covalent bond between two monomers (aas) between the C and N of the 2 adjacent monomers. Due to the sharing of the electrons, a peptide bond is a half double bond and thus doesnt rotate along the bond.
What is a polypeptide chain?
- Primary structure
- Starts with an amino group and ends with a carboxyl group (will be on exam)
- All starts with a Methionine/Met (AUG)
- Is important in determining how the protein folds and its function
What are the steps of protein folding?
- Primary structure -> polypeptide chain
- Secondary structure -> % alpha-helix, beta-pleated sheet, or neither
- Tertiary structure -> smaller interactions (ei H bonds, hydrophobic ints) depending on the polarity of the protein. Determines final folding.
What does the primary structure of a protein determine?
It determines how the protein folds and its function