Proteins 2 Structure Of Proteins: Sacc

Front 1

chain of amino acids

Back 1

Primary structure

Front 2

A protein structure that folds due to hydrogen bonding

Back 2

secondary

Front 3

order in which amino acids are covalently linked toether

Back 3

primary structure

Front 4

t/f: disulfide bonds is considered to be a part of primary structure

Back 4

False: Disulfide bonds are found in tertiary

Front 5

arrangement in space of the atoms in peptide backbone

Back 5

secondary structure

Front 6

it has repetitive interactions resulting from h-bonding b/w amide and carbonyl groups

Back 6

secondary

Front 7

The three types of secondary structure

Back 7

alpha helix

beta pleated sheets arrangement

collagen triple helix

Front 8

independently folded portions of proteins

Back 8

super secondary structure

Front 9

"motif"

Back 9

super secondary structure

Front 10

includes the side chains and prostetic groups

Back 10

tertiary structure

Front 11

arrangement of subunits with respect to one another

Back 11

quaternary structure

Front 12

aka multiple polypeptide chains of proteins

Back 12

subunits

Front 13

interaction b/w subunits is mediated by what type of interaction

Back 13

non-covalent bond

Front 14

what structure is associated with sickle cell anemia

Back 14

primary structure (change in one amino acid residue in the sequence)

Front 15

what type of bonds are polypeptide bonds

Back 15

amide bonds

Front 16

t/f: the bonds b/w the carbonyl group and the amide group can rotate

Back 16

false: they can't... due to partial double bond character

Front 17

t/f: the bonds coming from alpha carbon can rotate

Back 17

true

Front 18

used for determining angles where secondary stuctures will form

Back 18

ramachandran diagram

Front 19

ccw angle of rotation around N-C bond

Back 19

Phi

Front 20

CW angle of rotation around C-C bond

Back 20

Psi

Front 21

angle of the figure formed by two intersecting planes

Back 21

dihedral angle

Front 22

local folding of the polypeptide

Back 22

secondary structure

Front 23

Helical conformation stabilized by H-bond

Back 23

alpha helix

Front 24

t/f: proline creates a bend in the backbone because of its cyclic structure

Back 24

T (proline can not form alpha helix)

Front 25

what type of attraction occurs in alpha helix H-bond

Back 25

intramolecular

Front 26

in alpha helix, the r-group is projected inward

Back 26

F: outward to avoid crowding

Front 27

Keratin is an example of _____

Back 27

Alpha helix

Front 28

How many strands are involved in beta pleated sheets

Back 28

2 or more

Front 29

T/F: The Hydrogent bond is perpendicular to the polypeptide chain

Back 29

T

Front 30

what type of attraction occurs in Beta pleated sheet H-bond

Back 30

Intermolecular and intramolecular

Front 31

for B-pleated sheets, Which is more stable?

Anti-parallel or Parallel H-bond

Back 31

Anti-Parallel

Front 32

beta pleated sheet:

C-N alignment of H-bond (opposite direction)

Back 32

Anti-Parallel

Front 33

beta pleated sheet:C-C or N-N alignment of H-bond (same direction)

Back 33

Parallel

Front 34

silk and web is an example of what?

Back 34

beta pleated sheet

Front 35

T/F: G and P are frequently encountered in reverse turn (beta pleated sheet)

Back 35

T

Front 36

ability of polypeptide chains to foldback on itself or change direction

Back 36

reverse turn

Front 37

designs higher that secondary structure

Back 37

supersecondary structure

Front 38

bones and connective tissues component

Back 38

collagen

Front 39

how many strands are found in collagen triple helix

Back 39

3 strands

Front 40

repeating sequence in collagen triple helix

Back 40

X-P-G

X-Hydroxyproline-G

(X= any amino acid)

Front 41

most abundant protein

Back 41

collagen

Front 42

collagen triple helix is made up of 20% _______

Back 42

proline

Front 43

collagen is both intramolecularly and intermolecularly linked by covalent bonds.

formed by reactions of what two amino acids?

Back 43

H and K

Front 44

Keratin and collagen are both globular proteins

Back 44

F: fibrous

Front 45

two types of protein conformation

Back 45

Fibrous and globular

Front 46

protein conformation that is water soluble and has compact structure

Back 46

globular

Front 47

overall shape of globular proteins

Back 47

more or less spherical

Front 48

overall shape of fibrous proteins

Back 48

long and narrow rod

Front 49

the three dimentional arrangement of all atoms in a molecule

Back 49

tertiary structure

Front 50

the position of _______ and ________ are given emphaasis in the tertiary structure

Back 50

sidechains and prosthetic grooups

Front 51

structure that describes the conformation of the backbone

Back 51

secondary structure

Front 52

structure that describes the interaction of subunits

Back 52

quaternary structure

Front 53

t/f: non-polar residues cluster together in the interior of the in the interitior of the protein molecules as a result of ionic interaction

Back 53

hydrophobic interaction

Front 54

what type of attraction occurs between oppositely charged groups?

Back 54

electrostatic attraction:

this results in the groups being close together.

Front 55

what type of bonds are formed between the side chains of cysteines?

Back 55

disulfide bonds

Front 56

T/F: trypsin and chymotripsin contain sulfide bond

Back 56

t

Front 57

which amino acid is not found in an alpha helix?

Back 57

proline... it bends the chain

Front 58

the experimental technique used to determine the tertiary structure of a protein

Back 58

X-ray crystallography

Front 59

what is the conformation of myoglobin

Back 59

globular

Front 60

how many amino acid residues make up myoglobin

Back 60

153

Front 61

the prosthetic group found in the myoglobin and hemoglobin

Back 61

heme

Front 62

how many alpha helical regions can be found in the myoglobin?

Back 62

8

Front 63

how many beta pleated sheet can be found in myoglobin

Back 63

0

Front 64

T/F: 50% of the amino acid residues in myoglobin can be found in the alpha helical regions

Back 64

f: 75%

Front 65

_______ residues are found in the exterior ;

_______ residues are found in the interior

(polar, non-polar)

Back 65

polar- exterior

non-polar- interior

Front 66

t/f: the heme group does not affect the overall conformation of the myglobin.

Back 66

f

Front 67

the large organic ring in myoglobin

Back 67

protoporphyrin IX

Front 68

the oxidation number of the iron in the heme group

Back 68

2+

Front 69

structure of the protoporphyrin

Back 69

square planar

Front 70

what is the function of the myoglobin

Back 70

to store O2 in the Muscle

Front 71

how many coordination sites are present are present in the heme?

Back 71

6

Front 72

which amino acid is attached to the heme group

Back 72

Histidine f8

Front 73

how much is the afinity of CO to the myglobin greater than O2

Back 73

25000

Front 74

the term for oxygenated myglobin

Back 74

oxymyoglobin

Front 75

which amino acid serves as gate for the heme group

Back 75

his E7

Front 76

what would happen to Fe2+ if His E7 is not present?

Back 76

CO will bind to it

It will be oxidized to Fe 3+

Front 77

5 interactions found in tertiary structures

Back 77

h-bond

disulfide bonds

hydrophobic bonds

metalic bonds

ionic bonds

Front 78

name:

2 subunits-

3 subunits-

4 subunits-

3 identical subunits-

4 different subunits-

Back 78

2 subunits- dimer

3 subunits- trimer

4 subunits- tetramer

3 identical subunits- homotrimer

4 different subunits- heterotetramer

Front 79

proteins that have drastic changes in properties of one site due to to subtle changes in a distant site

Back 79

allosteric

Front 80

T/F: Hemoglobin is an allosteric protein

Back 80

T

Front 81

how many subunits are present in hemoglobin

Back 81

4 (tetramer)

Front 82

how many oxygen molecules can a myoglobin hold?

Back 82

1

Front 83

how many oxygen molecules can hemoglobin hold?

Back 83

4

Front 84

a cooperative effect whereby binding of the first ligand to an enzyme causes affinity for the next ligand to be higher

Back 84

positive cooperativity

Front 85

the shape of the oxygen binding curve for myoglobin

Back 85

hyperbolic

Front 86

the shape of the oxygen binding curve of myoglobin

Back 86

hyberpbolic

Front 87

which has higher percentage of saturation?

Mb or Hb

Back 87

Mb

Front 88

What is the function of the hemoglobin?

Back 88

to transport O2

Front 89

where in the lungs must hemoglobin bind oxygen for transport to the tissues

Back 89

alveoli

Front 90

oxygen pressure in the alveoli:______

oxygen pressure in the capillaries of active muscles:_______

Back 90

alveoli: 100 torr (Hb is 100% saturated)

capillaries: 20 torr (Hb is <50% saturated)

Front 91

The efffect of H+ in the affinity of Hb for oxygen

Back 91

Bohr efffect

Front 92

t/f: The Oxygen binding affinity of myoglobin is affected by the presence of H+

Back 92

F

Front 93

lower ph ________ the affinity of hemoglobin to oxygen

Back 93

decreases

Front 94

The oxygenated form of Hb is (stronger, weaker) acid

Back 94

stronger

Front 95

effect of 2,3-Bisposphoglycerate to O2 Affinity

Back 95

decreases O2 affinity

Front 96

effect of temperature to O2 affinity

Back 96

high temp; lower affinity

Front 97

state of hemoglobin when it is completely deoxygenated

Back 97

T-state "tense"

Front 98

state of hemoglobin when it is fully oxygenated

Back 98

R-staare "relaxed"