organization structure of proteins

Question 1

sequencce of amino acids

Answer 1

primary structure

Question 2

it gives identity to protein

Answer 2

sequence of amino acids

Question 3

what are the structures?

Answer 3

primary, secondary, tertiary, quaternary

Question 4

alpha-helix, beta-pleated sheet, triple helix

Answer 4

secondary structure

Question 5

simple molecules

Answer 5

quaternary structure

Question 6

how many molecules in hemoglobin

Answer 6

four (2 alpha and 2 beta)

Question 7

hemoglobin has this structure that binds to what?

Answer 7

hemistructure; iron (gives capacity as oxygen transporter)

Question 8

it affects other levels of protein structural organization

Answer 8

primary structure

Question 9

primary structure involves only the ______ linking residues together

Answer 9

covalent bonds

Question 10

the minimum size of a protein is defined as about ____ residues; smaller chains are referred to simply as _____. So the primary structure of a small protein would consist of a sequence of ____ or so residues

Answer 10

50; peptides; 50

Question 11

how many molecular weight per residue?

Answer 11

110 Da (daltons)

Question 12

largest protein discovered has how many residues and daltons/mweight?

Answer 12

30k residues and 3 million Da

Question 13

insulin has how many amino acids?

Answer 13

51

Question 14

what is the linkage for cysteine to cysteine?

Answer 14

disulfide linkage

• intramolecular if within one amino only
• intermolecular if with another amino acid

Question 15

largest known protein

Answer 15

titin or connectin

Question 16

is found in the striated muscle tissue of humans and other vertebrates

Answer 16

titin or connectin

Question 17

human titin is >1 µm long and consists of ___ folded protein domains

Answer 17

244

Question 18

Adults’ bodies contain ≈ __ g of titin.

Answer 18

500g

Question 19

who identified the sequence of insulin?

Answer 19

frederick sanger

Question 20

insulin has how many disulfide linkages?

Answer 20

three (1 intra and 2 inter)

Question 21

what is the structure of insulin?

Answer 21

tertiary structure

Question 22

the ____ structure of proteins can be characterized as a regular _____ structure held together by _____ bonding between the O of the___ and the H of the ____ groups in the polypeptide chains

Answer 22

secondary; three-dimensional, hydrogen, carbonyl (C=O), amino (NH)

Question 23

two examples of secondary structure

Answer 23

a-helical and b-pleated-sheet structures

Question 24

shape or conformation of a protein molecule

Answer 24

tertiary structure

Question 25

combination of secondary structure

Answer 25

tertiary structure

Question 26

what are the interactions in tertiary structure?

Answer 26

disulfide bonding hydrogen bonding ionic bonding hydrophobic attractions

Question 27

known also as the salt-bridge

Answer 27

ionic bonding

Question 28

positive ionic bonding is

Answer 28

basic amino acids (Arg, Lys, His)

Question 29

negative ionic bonding

Answer 29

acidic amino acids (aspartic and glutamic acids)

Question 30

nonpolar amino acids have what

Answer 30

hydrophobic attractions

Question 31

attraction between negatively and positively charged substituents on the R-groups

Answer 31

ionic bonding

Question 32

electrostatic attractions between COO- and N+ on acidic and basic side groups

Answer 32

ionic bonding

Question 33

Can occur between side chains that contain a hydrogen donor

Answer 33

hydrogen bonding

Question 34

occurs between a residue with an OH or NH and a residue with C = O, COOH, OH or NH

Answer 34

hydrogen bonding

Question 35

May be intermolecular of intramolecular

Answer 35

hydrogen bonding and disulfide linkage

Question 36

Can form between the –SH groups of two cysteine amino acids

Answer 36

disulfide linkages

Question 37

greater attraction than h-bonding

Answer 37

disulfide linkages

Question 38

Can exist between the Rgroups of nonpolar amino acid residues

Answer 38

hydrophobic attractions

Question 39

what is the bond in disulfide linkages

Answer 39

covalent bond

Question 40

a misnomer

Answer 40

hydrogen bonding

Question 41

in aqueous media, the chain folds so that the hydrophobic side chains face toward the interior, away from the outside environment of polar water molecules

Answer 41

hydrophobic attractions

Question 42

the hydrophobic groups associate together, strengthening the attractive dispersion forces and minimizing the possibility of a water molecule coming between them

Answer 42

true

Question 43

hydrogen bonding only occurs in?

Answer 43

O to H

Question 44

it determines the tertiary structure of insulin

Answer 44

disulfide bonding

Question 45

to manipulate the tertiary structure of hair protein

Answer 45

redox reaction

Question 46

loss of hydrogen, loss of electron, gain of oxygen

Answer 46

oxidation

Question 47

gain of hydrogen, gain of electron, loss of oxygen

Answer 47

reduction

Question 48

it breaks down disulfide linkages

Answer 48

reducing agent

Question 49

it binds the disulfide linkages again

Answer 49

oxidizing agent

Question 50

some complex proteins with two or more polypeptide chains can have what is known as __________

Answer 50

quaternary structure

Question 51

same forces and bonds that create tertiary structure also hold subunits together (quaternary) in a stable complex to form the _____ protein

Answer 51

complete protein

Question 52

some proteins are composed of more than one polypeptide chain

Answer 52

quaternary structure

Question 53

refers to the number and arrangement of the individual polypeptide chains

Answer 53

quaternary structure

Question 54

each polypeptide is referred to as a ______ of the protein

Answer 54

subunit

Question 55

_______ is a tetramer containing two pairs of non-identical (but similar) subunits. It has 2 α subunits and 2 β subunits

Answer 55

hemoglobin

Question 56

substance inside red blood cells that binds to oxygen in the lungs and carries it to the tissues (contains iron)

Answer 56

heme

Question 57

classify the bonds in each protein structure

Answer 57

primary: covalent bond secondary: hydrogen bonding tertiary and quaternary: hydrogen bonding, disulfide linkages, ionic bonding, and/or hydrophobic attraction

Question 58

are proteins that have a fiber-like shape

Answer 58

fibrous proteins

Question 59

Fibrous proteins serve as _____ supports and tend to be water ________

Answer 59

structural, insoluble

Question 60

a fibrous protein found in tendons, ligaments, and bone matrix

Answer 60

collagen

Question 61

what bond holds a-keratin?

Answer 61

disulfide bonding/linkage

Question 62

keratin is a ___ protein

Answer 62

fibrous

Question 63

fibroin forms what?

Answer 63

silk (fibroin is also a fibrous protein)

Question 64

proteins where the polypeptide chains are folded in a spherical or globular shape

Answer 64

globular proteins

Question 65

Globular proteins tend to be water ____- and can act as binding agents, enzymes, and as transport vehicles within the ___

Answer 65

soluble, binding agents, enzymes, transport vehicles, blood

Question 66

what are the four important globular proteins?

Answer 66

carboxypeptidase A, myoglobin, hemoglobin, immunoglobulin G

Question 67

myoglobin functions as a binding protein carrying _____ for muscle tissue

Answer 67

oxygen

Question 68

small enzyme that catalyzes protein digestion in the small intestine

Answer 68

carboxypeptidase A

Question 69

these proteins bind molecules that are foreign to the body, as a defense against disease

Answer 69

immunoglobulin g

Question 70

heme is a what group?

Answer 70

a prosthetic group

Question 71

present in proteins that have oxygen

Answer 71

heme

Question 72

oxygen-hemoglobin binding process, amount of oxygen/s in the cycle

Answer 72

0 1 4 3 0 starting, 1 will add 1 added, 3 more adds (oxygen binding) 4 added, 1 will remove 3 present, 3 will be released

Question 73

Some proteins contain polypeptide molecules associated with molecules or ions other than polypeptides

Answer 73

conjugated proteins

Question 74

hemoglobin includes the molecule ____ and the ion ____ in addition to the polypeptide molecule

Answer 74

heme and Fe2+ (iron)

Question 75

nonpolypeptide molecules are referred as what?

Answer 75

prosthetic groups

Question 76

proteins containing prosthetic groups are

Answer 76

conjugated proteins

Question 77

proteins without prosthetic groups are

Answer 77

simple proteins

Question 78

good cholesterol

Answer 78

high density lipoprotein (lipid carrier)

Question 79

what are the different classes in conjugated proteins?

Answer 79

glycoprotein, lipoprotein, nucleoprotein, hemoprotein, metalloprotein, phosphoprotein

Question 80

gamma globulin, mucin, interferon

Answer 80

glycoprotein

Question 81

hemoglobin, myoglobin

Answer 81

hemoprotein

Question 82

vldl, ldl, hdl

Answer 82

llipoprotein

Question 83

fe and zn

Answer 83

metalloprotein

Question 84

rna-bound protein

Answer 84

nucleoprotein

Question 85

casein

Answer 85

phosphoprotein