Amino acids

Question 1

Non polar aliphatic

Answer 1

hydrophobic (not glycine,, side chain too small), contribute to protein stability via hydrophobic intreactions with eachother

Question 2

Aromatic

Answer 2

Relativly non polar, hydrophobic, absorbs uv 280 nm

Question 3

Polar, uncharched

Answer 3

relativly hydrophilic, can form hydrogen bonds, covalent bonds

Question 4

positivly/ negativly charged groups

Answer 4

hydrophilic

Question 5

amino acids and bases

Answer 5

Amino group, carboxyl group and
ionizable R groups function as weak
acids and bases

Question 6

pI or isoelectric point

Answer 6

pH at which no net electric charge is present

Question 7

peptides

Answer 7

chains of amino acids, Side chains (R) contribute to acid-base
properties of the peptide,

Question 8

peptide bonds

Answer 8

➢ɸ (Phi): N-Cα (flexible)
➢ψ (Psi): Cα-C (flexible)
➢ω (Omega): C-N (not)

Question 9

alpha helix

Answer 9

right handed turn, R-groups outward, optimal use hydrogen bonds (not pro and gly) (hair feather nails)

Question 10

beta-conformations

Answer 10

parallel and antiparalel, R-groups protrude from opposite directions (silk fibrion)

Question 11

beta- turn

Answer 11

Connective elements linking successive  helices or  conformation
* 180 turn involving 4 amino acid residues
* Residue bias: Gly and Pro occur often
(collagen, bone matrix)

Question 12

tertiary structure

Answer 12

single type of secondary structures, suport protection, insoluable -> hydrophobic

Question 13

fold/motif

Answer 13

A recognizable folding pattern involving two or more elements of
secondary structures and the connections

Question 14

domain

Answer 14

A polypeptide chain as a single entity with respect to the entire
protein (with a specific function)
Structure of proteins