Peptide bonds

What’s Dipeptide mean

Have two amino acid units

What does tripeptide mean

has 3 AA residues

What does Oligopeptide mean

Up to 20 AA residues

What does Polypeptide mean

Over 20 AA residues

What Is special about peptide bonds

They aren’t easily broken, and have a short double bond that prevents free rotation

Which amino acids are cleaved by Trypsin

Lysine, Arinine

which amino acids does chymotrypsin cleave

Phenylalanine, tyrosine, and tryptophan

How are amino acids named

N-terminal to C-terminal

What special about the primary structure

It’s the OG structure and most important

What’s interesting about the secondary structure

alpha helix or beta sheet which makes parallel or antiparallel sheets

What’s special about tertiary structure

It helps with the domain where they’re attached

What’s special about the quaternary structure?

It takes multiple tertiary’s to make quaternary structure

What is the alpha heilx

Spiral structure that is stabilized by hydrogen bonding

What’s special about Proline’s structure

It’s a ridged cyclic structure that isn’t compatible with the spiral structure

Where are b-sheets common

Globular proteins

What is the -d structural unit of a polypeptide

Domains, as they the fundamental functional strucutre

How many amino acids does it take for a domain

Polypeptides chain with 200+ amino acids make 2+ domains

What makes and breaks a disulfide bond

reduction break, oxidation creates

What is the worst part of denaturation

It’s irreversible

What is a chaperone

It’s a specified protein that is needed for proper folding

what are subunits

Basically pieces that are attached via non-covalent or covalent interactions to form quaternary structure