Cell Biology

Front 1

What was the first protein sequenced directly by Amino Acid sequencing methods?

Back 1

Insulin

Front 2

How many amino acid are in an average protein molecule?

Back 2

50-2000

Front 3

Single chain of amino acid less than 50 AA long?

Back 3

peptide

Front 4

single chain of AA greater than 50 AA long?

Back 4

polypeptide

Front 5

functional unit of one or more polypeptides or peptides?

Back 5

protein

Front 6

How many AA are produced from one turn of the alpha helix?

Back 6

3.6 AA

Front 7

What type of bonds stabilize an alpha helix?

Back 7

Hydrogen bonds

Front 8

What is the name for a single polypeptide chain coiled into a cylinder?

Back 8

Alpha Helix

Front 9

What type of bond forms beta sheets?

Back 9

Hydrogen Bonds

Front 10

What is it called when a beta sheet runs in the same orientation?

Back 10

Parallel

Front 11

What is it called when a Beta sheet runs in opposite directions?

Back 11

Anti-parallel

Front 12

Regions of polypeptide chains that are not involved in alpha helix coiling or beta sheets are said to have what?

Back 12

Random Coiling

Front 13

Random coiling is what type of structure?

Back 13

Secondary structure

Front 14

What is the term used for alpha helices that wrap or coil around each other?

Back 14

Coiled Coil

Front 15

In random coiling hydrophobic side chains interact with each other in which part of the structure?

Back 15

Center

Front 16

What is a part of a polypeptide chain that can fold independently into a compact stable structure and is a modular unit from which many larger proteins are made?

Back 16

Protein Domain

Front 17

T or F: Large proteins can have many different domains that are connected by relatively unstructured regions of a polypeptide chain.

Back 17

True

Front 18

groups of proteins with similar structures and sequences.

Back 18

Protein Families

Front 19

Any part of a proteins surface that interacts with another molecule through non-covalent bonds.

Back 19

Binding Site

Front 20

T/F A globular protein is an individual polypeptide chain that binds together to form a functional protein.

Back 20

False; Subunit

Front 21

Two identical polypeptides binded together.

Back 21

Dimers

Front 22

If a binding site on a protein binds to same site on another copy of that same protein then what will form?

Back 22

Dimers

Front 23

What does it mean with it is said that a protein can self assemble?

Back 23

When you disassociate the complex of bound proteins into subunits that they can then self assemble themselves.

Front 24

What is the significance of proteins self assembling?

Back 24

Means all info chemically needed for assembly of complex structure is present in subunits.

Front 25

Of the two main types of proteins, which ones are rounded up with irregular surface and consists of most proteins?

Back 25

Globular Proteins

Front 26

Of the two main types of proteins, which ones are elongated?

Back 26

Fibrous Proteins

Front 27

Is collagen an example of a globular protein or a fibrous protein?

Back 27

Fibrous Proteins

Front 28

Many extracellular proteins may have their structures stabilized by one type of covalent bond known as what type bond?

Back 28

Di-Sulfide Bond

Front 29

Where do Di-Sulfide bonds form on extracellular proteins?

Back 29

between adjacent Cysteine Amino Acids

Front 30

Where are di-sulfide bonds catalyzed?

Back 30

Endoplasmic Reticulum

Front 31

What is it about a protein that gives it its unique function?

Back 31

Its shape

Front 32

What is a binding molecule called?

Back 32

Ligand

Front 33

What are binding sites made of?

Back 33

Amino Acid R-groups

Front 34

What anchors membrane proteins?

Back 34

Hydrophobic alpha helices

Front 35

Antibodies are produced in response to what?

Back 35

Antigens(foreign molecules)

Front 36

"Y" shaped with two identical antigen binding sites.

Back 36

Antibodies

Front 37

Antibodies that bind to different antigens can be created by changing what?

Back 37

Length and amino acid sequence of loops.

Front 38

Higher number of weak bonds in antibodies means

Back 38

higher affinity and higher specificity

Front 39

a variety of antibodies that binds antigens in different ways

Back 39

Polyclonal Antibodies

Front 40

How are monoclonal antibodies formed

Back 40

by fusing b-cells with a b tumor cell

Front 41

how is strength of binding measured and represented?

Back 41

Equilibrium constant

Front 42

In equilibrium constant if the binding strength gets increased is the free energy negative or positive?

Back 42

negative and K gets larger

Front 43

enzymes increase what?

Back 43

reaction rates

Front 44

what do nucleases catalyze?

Back 44

hydrolysis of nucleic acids

Front 45

What do synthases catalyze?

Back 45

condensing of small molecules into larger molecules

Front 46

What do kinases catalyze?

Back 46

addition of phosphate functional groups

Front 47

What does lysozyme catalyze?

Back 47

the splitting of polysacharide chains in bacterial cell walls, causing the cell to lyse/die

Front 48

What was the first enzyme with xray crystallography?

Back 48

Lysozyme

Front 49

What does the lysozyme active site look like?

Back 49

long groove that holds six linked sugars

Front 50

What provides a localized increase in availability of protons in a lysozyme active site?

Back 50

glutamic acid r-group

Front 51

Low Km means what?

Back 51

concentration of substrate at which the enzyme works at its half maximal speed(Vmax)indicates the substrate binds very tightly.

Front 52

How many heme groups does hemoglobin have?

Back 52

Four

Front 53

What type of chromatography deals with positively or negatively charged molecules stuck to beads to slow down protein molecules of opposite charge?

Back 53

Ion Exchange Chromatography

Front 54

What type of Chromatography has beads with small holes in them that slow down proteins that are small enough to fit inside the holes and larger molecules move quicker?

Back 54

Gel Filtration Chromatography

Front 55

What type of chromatography deals with beads that bind specifically to the protein of interest

Back 55

Affinity Chromatography

Front 56

What type of Chromatography uses hydrophobicity?

Back 56

Reverse Phase Chromatography

Front 57

What is a highly computerized form of chromatography in which small beads are run under high pressure?

Back 57

High Performance Liquid Chromatography

Front 58

Method in which proteins are subjected to an electric field they migrate in a direction and speed that reflects their net charge and size

Back 58

Gel Electrophoresis

Front 59

What does PAGE stand for?

Back 59

Poly Acrylamide Gel Electrophoresis

Front 60

What does SDS PAGE do to proteins?

Back 60

Denatures proteins and gives them constant negative charge to mass ratio

Front 61

In SDS-PAGE when the mixture is applied to a slap the molecules will tend to do what?

Back 61

Migrate to their anode according to their molecular weight

Front 62

SDS-PAGE allows for an estimate of what?

Back 62

molecular weight and minimum subunit number

Front 63

In Isoelectric focusing, when you apply the current, proteins will migrate thru the gel until they reach a pH at which they no longer have a net charge. What is this point called?

Back 63

Isoelectric Point

Front 64

Isoelectric focusing separates by what?

Back 64

Charge

Front 65

2-D PAGE combines what two methods?

Back 65

SDS-PAGE and Isoelectric Focusing

Front 66

What was the first Amino Acid sequenced?

Back 66

Insulin

Front 67

In Edmond degradation what terminal end is cleaved off?

Back 67

N-Terminal end

Front 68

Single stranded DNA molecule that is used in hybridization reactions to detect nucleic acid molecules containing a complementary sequence

Back 68

DNA Probe

Front 69

What type of crystallography mathematically analyzes the xray diffraction pattern of spots that are created when a direct x-ray beam is shined through a solid crystal of pure protein

Back 69

X-ray crystallography

Front 70

Method in which protein is put in a strong magnetic field and subjected to radio frequency pulses of electromagnetic radiation.

Back 70

Nuclear Magnetic Resonance Spectroscopy

Front 71

What are the five functions of a membrane?

Back 71

1) Barrier 2) allows transport 3) detects external signals 4) site of certain enzymatic activites 5) Structural roles

Front 72

T/F Membranes change shape easily

Back 72

True

Front 73

Describe the structure of a membrane?

Back 73

2 sheets of lipid molecules that form a lipid bi-layer

Front 74

What is the definition for having both hydrophobic and hydrophilic parts?

Back 74

Amphipathic

Front 75

In a lipid bi-layer the heads are _______ and the tails are __________

Back 75

Hydrophilic, Hydrophobic

Front 76

What is the most abundant membrane lipid?

Back 76

Phospholipids

Front 77

What are four ways membranes are mobile?

Back 77

Lateral diffusion, rotation, flip flop and flexion.

Front 78

If you decrease the temp that will make the membrane more fluid. T/F

Back 78

False; Less Fluid

Front 79

T/F The longer the fatty acid tails in the membrane the less fluid the membrane will be.

Back 79

True

Front 80

T/F Less saturation means more double bonds between carbon tails which means less fluidity.

Back 80

False; more fluidity

Front 81

What type of cells alter the lengths of FA tails in response to changes in temperature to maintain constant fluidity?

Back 81

Bacteria and Yeast cells

Front 82

less cholesterol = increased or decreased fluidity?

Back 82

Increased

Front 83

Cholesterol ______ the membrane thus ________ fluidity and ________ permeability of the lipid bi-layer.

Back 83

stiffens, decreasing, decreasing

Front 84

T/F Cell membranes are very symmetrical.

Back 84

False; they are asymmetrical

Front 85

Where does phospholipid asymmetry actually occur?

Back 85

Endoplasmic Reticulum

Front 86

Enzyme that catalyzes transfer of lipid molecules to opposite monolayer.

Back 86

Flipases

Front 87

Where are glycolipids found?

Back 87

Plasma Membrane and the non-cytosolic face facing the outside environment

Front 88

Where does asymmetry of glycolipids occur?

Back 88

Golgi Apparatus

Front 89

glycolipids, unlike phospholipids, will always face cells exterior T/F

Back 89

True

Front 90

Does glucose diffuse fast or slow across bi-layer?

Back 90

Slow

Front 91

Transport or allow certain molecules across membrane

Back 91

Permeases

Front 92

type of membrane protein that provides structure

Back 92

linkers

Front 93

type of membrane protein that detects exterior signals and relays them to cells interior.

Back 93

receptors

Front 94

What is a transmembrane protein?

Back 94

a protein that passes all the way thru the bi-layer, exposed to a aqueous environment on each side

Front 95

Membrane proteins are usually very asymmetrical. T/F

Back 95

True

Front 96

What type of membrane protein is tightly associated w/ the membrane requiring detergents to disrupt the bi-layer in order to remove them from the membrane.

Back 96

Integral Membrane protein

Front 97

What membrane protein is not a Integral Membrane protein?

Back 97

Protein-attached membrane proteins

Front 98

How many AA's does it take to cross bilayer as double helix?

Back 98

20 or so

Front 99

transmembrane proteins that cross the bi-layeras a beta sheet structure curved into a cylinder is called what?

Back 99

Beta Barrel

Front 100

What is used to make a membrane protein completely soluble?

Back 100

Detergents

Front 101

In water, detergent molecules aggregate into what?

Back 101

spherical micelles

Front 102

What does bacteriorhodopsin do to a cell?

Back 102

pumps protons out of cell when it absorbs light energy

Front 103

What non-protein compound is in bacteriorhodopsin to pumps protons out of cells??

Back 103

Retinal

Front 104

How many subunits does bacterial photosynthetic reaction centers have?

Back 104

four

Front 105

In bacterial photosynthetic reaction centers, the fourth complex, cytochrome, is peripherally bound to what?

Back 105

the transmembrane subunits of the outer surface

Front 106

meshwork of fibrous proteins that determine the shape of the cell and the mechanical properties of the plasma membrane.

Back 106

Cell Cortex

Front 107

What is the cell cortex attached to?

Back 107

the cytosolic surface of the membrane

Front 108

What is the main component of the cell cortex?

Back 108

the protein spectrin

Front 109

The cell coat is made from proteins T/F

Back 109

False; Carbohydrates

Front 110

the carbohydrates that form the cell coat are located only where?

Back 110

Extracellular

Front 111

3 Functions of cell coat

Back 111

1) Protection 2) Lubricates 3) Provides cell identity markers

Front 112

At what site do specialized junctional proteins form a continuous belt around the cell where it contacts its neighbors, creating a seal between adjacent cell membranes.

Back 112

tight junction