F2 og F3. Protein struktur og analyse og Protein struktur og funktion

Question 1

Describe a competetive inhibitor that directly blocks substrate binding to an enzyme

Answer 1

Question 2

Give a few examples of some general functions

Answer 2

Question 3

Describe why A helix is a common, regular, biological structure

Answer 3

Question 4

Describe why a protein is made of amino acids linked togehter into a polypeptide chain

Answer 4

Question 5

Make a schematic model of how a motor protein uses ATP hydrolysis to move in one direction along a cytoskeletal filament

Answer 5

Question 6

Desciribe a series of enzyme-catalyzed reactions forms a linked pathway

Answer 6

Question 7

Explain how a single type of protein subunit can pack together to form a filament, a hollow tube, or a spherical shell

Answer 7

Question 8

Make a survey of nucleotides

Answer 8

Question 9

Explain acids

Answer 9

Question 10

Show how affinity chromatography can be used to isolate the binding partners of a protein of interest

Answer 10

Question 11

Show how all amino acids have an amino group, a carboxyl group, and a side chain (R) attached to their a-carbon atom

Answer 11

Question 12

Draw alpha and beta links

Answer 12

Question 13

Show alternating double bonds

Answer 13

Question 14

Show how amino acids are linked together by peptide bonds

Answer 14

Question 15

Show how Amino acids in a protein are held together by peptide bonds

Answer 15

Question 16

Show how An actin filament is composed of identical protein subunits

Answer 16

Question 17

Show how an antibody is Y-shaped and ahs two identical antigen-binding sites, one on each arm of the Y

Answer 17

Question 18

Show how an energetically unfavorable reaction can be driven by an energetically favorable follow on reaction that acts as a chemical siphon

Answer 18

Question 19

show how An enzyme’s performance depends on how rapidly it can process its substrate

Answer 19

Question 20

Explain bases

Answer 20

Question 21

Show how beta sheets can stack to form an amyloid structure

Answer 21

Question 22

Show how beta sheets come in two varieties

Answer 22

Question 23

show how Binding sites allow proteins to interact with specific ligands

Answer 23

Question 24

Breaking open cells and tissues

Answer 24

Question 25

show how carbon atoms cycle continuously through the biosphere

Answer 25

Question 26

Draw carbon skeletons

Answer 26

Question 27

Show how catabolic and anabolic pathways together constitue the cell's metabolism

Answer 27

Question 28

Draw C-H compunds

Answer 28

Question 29

Explain how changes in conformation can allow a protein to walk along a cytoskeletal filament

Answer 29

Question 30

Show how chaperone proteins can guide the folding of a newly synthesized polypeptide chai

Answer 30

Question 31

Draw C-N compounds

Answer 31

Question 32

Draw C-O compounds

Answer 32

Question 33

Draw complex oligosaccharides

Answer 33

Question 34

Explain covavlent bonds

Answer 34

Question 35

Show how Denatured proteins can often recover their natural shapes

Answer 35

Question 36

Draw di-, oligo- and polysaccharides

Answer 36

Question 37

Explain how Disulfide bonds help stabilize a favored protein conformation

Answer 37

Question 38

Explain electrostatic attraction in water.

Answer 38

Question 39

Draw electrostatic attractio

Answer 39

Question 40

Explain why Energetically favorable reactions have a negative DeltaG, whereas energetically unfavorable reactions have a positive DeltaG

Answer 40

Question 41

Show how enzymes bind to, and chemically alter, substrate molecuels

Answer 41

Question 42

Show how Enzymes can encourage a reaction in several ways

Answer 42

Question 43

Show how enzymes catalyze reactions by lowering the activation-energy barrier

Answer 43

Question 44

Show how enzymes convert substrates to products while remaining unchanged themselves

Answer 44

Question 45

Howcome even energetically favorable reactions require activation energy to get them started

Answer 45

Question 46

Explain fatty acids

Answer 46

Question 47

Explain how Feedback inhibition at multiple points regulates connected metabolic pathways

Answer 47

Question 48

Explain how Feedback inhibition regulates the fow through biosynthetic pathways

Answer 48

Question 49

Explain how Feedback inhibition triggers a conformational change in an enzyme

Answer 49

Question 50

Describe how Fibrous proteins collagen and elastin form very different structures

Answer 50

Question 51

Explain Free energy

Answer 51

Question 52

Make an overview over historical landmarks in our understanding of proteins

Answer 52

Question 53

Draw hydrogen bonds in water.

Answer 53

Question 54

Explain how Hydrogen bonds within a protein molecule help stabilize its folded shape

Answer 54

Question 55

Draw hydrogen bonds

Answer 55

Question 56

Draw a hydrogen ion exchange

Answer 56

Question 57

Draw hydrophilic molecules

Answer 57

Question 58

Show how hydrophobic forces help proteins fold into compact conformations

Answer 58

Question 59

Explain hydrophobic forces

Answer 59

Question 60

Draw hydrophobic molecules

Answer 60

Question 61

Explain how Identical protein subunits can assemble into complex structures

Answer 61

Question 62

Explain how Intertwined alpha helices can form a still coiled-coil

Answer 62

Question 63

Explain how intracellular condensates can form biochemical subcompartments in cells

Answer 63

Question 64

Draw isomers

Answer 64

Question 65

Explain how living cells do not defy the second law of thermodynamics

Answer 65

Question 66

Explain how lowering the activation energy greatly increases the probability that a reaction will occur.

Answer 66

Question 67

Explain how Lysozyme cleaves a polysaccharide chain

Answer 67

Question 68

Explain how many different GTP- binding proteins function as molecular switches

Answer 68

Question 69

Explain how Many protein molecules contain multiple copes of the same protein subunit

Answer 69

Question 70

Explain how Many proteins are composed of separate functional domain

Answer 70

Question 71

Explain how Many viral capsids are essentially spherical protein assemblies

Answer 71

Question 72

Explain how Mass spectrometry can be used to identify proteins by determining the precise masses of peptides derived from them

Answer 72

Question 73

Explain how Measured reaction rates plotted to determine the Vmax and Km of an enzyme-catalyzed reaction

Answer 73

Question 74

Draw monosaccharides

Answer 74

Question 75

Explain how Most proteins belong structurally related families

Answer 75

Question 76

Explain how oxidation and reduction involve a shift in the balance of electrons

Answer 76

Question 77

Explain pH.

Answer 77

Question 78

Explain phosphates

Answer 78

Question 79

Explain how photosynthesis and cell respiration are complementary processes in the living world

Answer 79

Question 80

Explain how Prion diseases are caused by proteins whose misfolding is infectious.

Answer 80

Question 81

Explain how Protein conformation can be represented in a variety of ways

Answer 81

Question 82

Explain how Protein machines can carry out complex functions

Answer 82

Question 83

Explain how Protein phosphorylation is a very common mechanism for regulating protein activity.

Answer 83

Question 84

Explain Protein separation by chromatrography

Answer 84

Question 85

Explain how Reaction coupling can drive an energetically unfavorable reaction

Answer 85

Question 86

Explain how Reactions will eventually reach a chemical equlibrium

Answer 86

Question 87

Explain how Retinal and heme are required for the function of certain proteins

Answer 87

Question 88

Explain how Ribbon models show these different protein domains

Answer 88

Question 89

Draw ring formation

Answer 89

Question 90

Explain how Scaffold proteins can concentrate interacting proteins in the cel

Answer 90

Question 91

Explain how Serine proteases constitute a family of proteolytic enzymes

Answer 91

Question 92

Explain how small changes in the number of weak bonds can have drastic effects on a binding interaction

Answer 92

Question 93

Explain how some chaperone proteins act as isolation chambers that help a polypeptide fold

Answer 93

Question 94

List some common functional classes of enzymes

Answer 94

Question 95

Explain how some polypeptide chains fold into an orderly pattern called a beta sheet

Answer 95

Question 96

Explain how Some polypeptide chains fold into an orderly repeating form known as an alpha helix

Answer 96

Question 97

Explain how Some proteins are formed as a symmetrical assembly of two different subunits

Answer 97

Question 98

Explain how Spherical, liquid-drop-like nucleoli can be seen to fuse in the light microscope

Answer 98

Question 99

Draw sugar derivatives

Answer 99

Question 100

Draw sulfhydryl groups

Answer 100

Question 101

Explain the amino acids found in proteins

Answer 101

Question 102

Explain the antibody molecule

Answer 102

Question 103

Explain why the binding of a protein to another molecule is highly selective

Answer 103

Question 104

Explain how The binding of a regulatory ligand can change the eqilibrium between two protein conformations

Answer 104

Question 105

Explain why The equilibrium constant, K, for the reaction A+B ---\> AB depends on the concentrations of A, B and AB

Answer 105

Question 106

Explain how The modification of a protein at multiple sites can control the protein's behavior

Answer 106

Question 107

Explain how three types of noncovalent bonds help proteins fold

Answer 107

Question 108

Explain the Twenty different amino acids are commonly found in proteins

Answer 108

Question 109

Explain van der waals attractions

Answer 109

Question 110

Explain water as a solvent

Answer 110

Question 111

Draw and explain water.

Answer 111

Question 112

Explain weak noncovalent chemical bonds

Answer 112

Question 113

Explain x-ray crystallography

Answer 113