Levels of Protein Structure
Protein Structure Basics
Protein Folding
Protein Function
Protein Control
DNA Structure
Techniques in Cell Biology
Functional Groups
Chromosomes
Lipid membranes
100

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

primary

100

These are the building blocks of proteins

amino acids

100

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

hydrophobic forces

100

What is one thing that can induce conformational changes within proteins?

pH, temperature, interaction with other molecules

100

This covalent modification acts like an on/off switch for some proteins

phosphorylation

100

These are the 3 components of a nucleotide

deoxyribose sugar, phosphate group, nitrogenous base
100
This type of microscopy uses visible light shining through transparent cells

Light Microscopy

100

This functional group contains an oxygen and a hydrogen

Hydroxyl

100

This is the center of the chromosome that is bound by the mitotic spindle during the cell cycle to help separate sister chromatids

Centromere

100

This type of lipid composes cell membranes

Phospholipids

200

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

secondary

200

These covalent bonds hold amino acids together

peptide

200

These proteins assist with polypeptide folding

chaperone proteins
200

This portion of an antibody binds to its antigen

variable portion

200

This enzyme phosphorylates proteins

kinase

200

These two nucleotides are purines

adenine and guanine

200

This type of microscopy uses UV light to visualize cells

Fluorescent microscopes

200

This functional group contains a carbon double bonded to and oxygen

Carbonyl

200

This structure is composed of histones, non-histone proteins, and DNA

Chromatin

200

This type of membrane protein fully spans the bilayer

Transmembrane protein

300

This is the most common type of secondary structure

alpha helices

300

Amino acids have these 4 general features

alpha carbon

amino group

carboxyl group

R group/side chain

300

An abnormal form of a protein is called this

a prion

300

This is how enzymes speed up reactions

by lowering activation energy

300

GTP-binding proteins are switched on when this happens

GTP binds to the protein

300

This is the covalent bond that connects nucleotides

phosphodiester

300

This type of microscopy passes electrons through a sample to produce a 2D image

Transmission electron microscopy (TEM)

300

This functional group contains a nitrogen and 2 hydrogens

Amino
300

Structural maintenance of chromosome proteins use this to power higher order chromosome organization

ATP hydrolysis

300

These 3 things increase membrane fluidity

Higher temperature

More double bonds

Shorter phospholipid tails

400

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

tertiary

400

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

R group or side chain

400

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

beta sheet

400

This is reached when all enzymes are occupied by a substrate

VMAX

400

This molecule accelerates the release of GDP from a G-protein

Guanine nucleotide exchange factor (GEF)

400

This is the shape that double stranded DNA forms

double helix

400

This technique shoots x-rays at a crystal, producing a diffraction pattern that can be used to determine structure

X-ray crystallography

400

This functional group contains a sulfur and a hydrogen

Sulfhydryl

400

This SMC protein creates topologically associated domains during chromosome packing

Cohesin

400

This enzyme moves phospholipids from the extracellular side of the membrane to the cytosolic side

Flippase

500

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

quaternary

500

Amino acids link together to form what?

a polypeptide chain

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

500

These are the 3 ways enzymes chemically transform their substrates

1. correct orientation

2. rearrange electrons

3. strain the substrate

500

This molecule prevents the release of GDP from a G-protein

Guanine nucleotide dissociation inhibitor (GDI)

500

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

C and G: 3

A and T: 2

500

This type of microscopy bounces electrons off the surface of a sample to produce a 3D image

Scanning electron microscopy (SEM)

500

This functional group contains a carbon, a double bonded oxygen, and a hydroxyl

Carboxyl

500

These proteins make up the nucleosome core along with DNA. Be sure to name all 4!

H2A, H2B, H3, H4

500

These are membrane-less compartments that concentrate proteins or nucleic acids and are found across all life forms

Biomolecular condensates