BIOL302 Unit 1 Exam

Levels of Protein Structure

100

This level of structure is determined by the amino acid sequence of a polypeptide

primary

200

This level of amino acid structure is determine by hydrogen bonding along the polypeptide backbone

secondary

300

This is the most common type of secondary structure

alpha helices

400

This level of amino acid structure is due to the properties of amino acids that contribute to a polypeptides 3D structure

tertiary

500

This level of amino acid structure is caused by polypeptide subunits joining together

quaternary

Protein Structure Basics

100

These are the building blocks of proteins

amino acids

200

These covalent bonds hold amino acids together

peptide

300

Amino acids have these 4 general features

alpha carbon

amino group

carboxyl group

R group/side chain

400

This region of an amino acid gives it it's unique properties

R group or side chain

500

Amino acids link together to form what?

a polypeptide chain

Types of Proteins

100

You may find this kind of protein giving support to the cell membrane

structural protein

200

This type of protein helps speed up reactions

enzymes

300

This type of protein relays messages between cells

signal protein

400

This protein is responsible for detecting signals and making sure the message gets to the right place inside the cell

receptor proteins

500

This type of protein acts like a switch, turning genes on and off

gene regulatory protein

Amino Acids

100

What are the 1 and 3 letter abbreviations for Alanine?

A

Ala

200

What are the 1 and 3 letter abbreviations for Tryptophan?

W Trp

300

What are 3 of the polar amino acids?

Serine Threonine

Cysteine Asparagine

Glutamine Tyrosine

400

What are 3 of the charged amino acids?

Aspartate Glutamate

Lysine Arginine

Histidine

500

What are 3 of the nonpolar amino acids?

Glycine Isoleucine Proline

Alanine Methionine

Valine Phenylalanine

Leucine Tryptophan

Protein Folding

100

These forces help proteins compact into their conformation due to the aqueous environment of the cell

hydrophobic forces

200

These proteins assist with polypeptide folding

chaperone proteins

300

An abnormal form of a protein is called this

a prion

400

This secondary structure is held together by hydrogen bonds between amino acids above and below a plane

beta sheet

500

You would expect to find this kind of amino acid on the inside of an alpha helix that is crossing a phospholipid bilayer

polar or charged

How Proteins Work

100

This binds to a protein pocket with great specificity

ligand

200

This portion of an antibody binds to its antigen

hypervariable loops

300

This is how enzymes speed up reactions

by lowering activation energy

400

This is reached when all enzymes are occupied by a substrate

V_MAX

500

These are the 3 ways enzymes chemically transform their substrates

1. correct orientation

2. rearrange electrons

3. strain the substrate

Protein Control

100

This type of protein control is used to regulate metabolic pathways

feedback inhibition

200

This enzyme phosphorylates proteins

kinase

300

GTP-binding proteins are switched on when this happens

GTP binds to the protein

400

Motor proteins use this method to move along the cytoskeleton

AATP hydrolysis

500

This type of regulation involves the binding of a molecule to a site other than the active site of an enzyme

allosteric regulation

DNA Structure

100

These are the 3 components of a nucleotide

deoxyribose sugar, phosphate group, nitrogenous base

200

These two nucleotides are purines

adenine and guanine

300

This is the covalent bond that connects nucleotides

phosphodiester

400

This is the shape that double stranded DNA forms

double helix

500

How many hydrogen bonds join base pairs C and G AND A and T?

C and G: 3

A and T: 2