Amino Acids and Proteins Flashcards

1
Q

structural or mechanical roles, polypeptides are intertwined to form cables or fibers

A

fibrous proeins

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2
Q

are functional or nonstructural, chains folded on itself to give compact rounded structure and are water soluble

A

globular proteins

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3
Q

aspartate is

A

acidic amino acid

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4
Q

glutamate is

A

acidic amino acid

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5
Q

arginine

A

basic

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6
Q

lysine

A

basic

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7
Q

histidine

A

basic

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8
Q

nonpolar

A

glycine, alanine, leucine and phenylalanine

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9
Q

serine, cysteine, threonine and tyrosine

A

neutral

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10
Q

glycine, alanine, leucine and phenylalanine

A

nonpolar

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11
Q

what forms of amino acid are found in humans

A

L forms

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12
Q

sulfur containing amino acids

A

methioine and cysteine

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13
Q

aromatic compounds

A

phenylalanine, tyrosine, and tryptophan

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14
Q

nonpolar

A

glycine, alanine, proline, valine, leucine, and isoleucine

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15
Q

polar

A

asparagine, glutamine, serine and threonine

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16
Q

2 cysteins can spontaneously oxidize to produce

A

cystine via a disulfide bridge

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17
Q

__________is a genetic disease resulting in defective transport protein that reabsorbs cystine into renal tubular cells and apppears in urine and forms calculi

A

cystinuria

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18
Q

_______is the sequence of amino acids in a polypeptide chain

A

primary structure

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19
Q

peptide bond is

A

carboxyl end and amino acid

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20
Q

__________is the folding or coiling of the chain to give regular repeated motifs

A

secondary structure

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21
Q

intramolecular H-bonding

A

between different parts of the same chain

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22
Q

intermolecular H bondingq

A

between different chains

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23
Q

how are secondary structures stabilized

A

stabilized by hydrogen bonds formed between the carbonyl oxygen of one peptide bond and the amino hydrogen of another

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24
Q

intermoleclar hydrogen bonding and intramolecular hydrogen bonding

A

beta pleated sheet

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25
intramolecular hydrogen bonding
alpha helix
26
____________secondary structures is strong, non-elastic and flexible
beta pleated sheat
27
strong and may be elastic type of secondary structure
alpha helix
28
_______are strong rope like strucutres of intertwised alpha helices which are a major component of external protective layers in mammals
keratins
29
_______have high sulfur content and many S-S bonds
hard keratins
30
_______have low sulfur content and few S-S bonds between the chains
soft keratins
31
___________are a family of extracellular glycoproteins and are a major protein of connective tissue and forms insolbule fibers of great strength
collagnes
32
composition of collagens
rigid, cross linked triple helical rods
33
collagen has a high content of
glycine, proline, hydroxyproline and lysine
34
what two amino acids confer collagens rigidity
pro and hyp
35
what is the fundamental unit of collagen
tropocollagen
36
____________is a triple helical rod that is rigid and has a wider pitch than alpha helix to accomodate the bulky pro and hyp residues
collagen
37
________-is the modification of a structure after synthesis of the poypeptide chain
post-translational modification
38
_______ and ________ residues are hydroxylated
pro and lys
39
hydroxylated pro forms
h bonds between chains
40
hydroxylated lys forms
covalent bonds between chains
41
pro and lys residues become hydroxylated reuiqres
vitamin C
42
the collagen in tendons are arranged as
parallel bundles
43
the collagen in skin are arranged in
sheets of fibrils lyaered at many angles
44
the collagen in cartilage has
no distinct arrangement
45
cornea collagen is
planar sheats stacked corssways to minimize light scatter
46
_________is the overall 3d structure of the folded peptide
tertiary structure
47
globular proteins fold during and following synthesis along the same principles as
micell formation
48
what are some forces that can stabilize structures of globular proteins
electrostatic attractions hydrogen bonds hydrophobic interactions disulfide bonds
49
________assist in protein folding by slowing it down to prevent inapprorpiate interactions
molecular chaperones
50
_____________are protein conformational diseases caused by misfolded proteins
prion diseases
51
what protein structure is messed up in prion diseases
tertiary structure
52
_____________are domains that are physically independent regions within the overall tertiary structure of a large complex protein
structural domains
53
polymorphisms, protein families isoforms, and developmental variation are all examples of
variations in primary structure
54
_____________ are variations in primary structure of 2 or more alleles may be silent some have a profound effect
polymorphisms
55
_________-are proteins with simila but NOT identical structure and function that have evolved from the same ancestral protein; sequences very similar
protein families
56
examples of protein families
hemoglobin chains, myoglobin serine proteases
57
_____________perform essentially the same function and are highly homologus and evolved from the same ancestral gene possess different amino acid sequences and physico-chemical properties
protein isoforms
58
___________are different isoforms that are expressed during different stages of development
developmental variation
59
__________are highly similar sequences that evolved from the same ancestor
homologs
60
____________are from different species but orignated from same gene in ca common ancestor and normally retain same function
orthologs
61
example of orthologs
human bovine and procine insulin
62
___________from same species, originated from common ancestral gene, have different functions ( myogloin and different hemoglobin chains)
paralogs
63
fetal hb have what structure
alpha 2 gamma 2
64
adult hb have what structure
alpha 2 beta 2 or alpha 2 delta 2
65
gower I
zeta 2 epsiolon 2
66
gower II
alpha 2 epsiolon 2
67
protalnd I
zeta 2 gamma 2
68
________is the aggregation of an interaction between subunits in a multimeric protein
quatenary structure
69
human hemoglobin differences are examples of
paralogs
70
does myoglobin have a higher or lower affinity for oxygen
myoglobin
71
in the absence of oxygen hemoglobin is predominantly in the
T state
72
when oxygen binds all four subunits change to the ________ state
R state
73
binding of myoglobin is
noncooperative so graph is hyperbolic
74
at a lower pH Hb has a
less affinity for the oxygen
75
fetal red blood cells have
higher affinity for oxygen than maternal RBC's
76
2,3 BPG and carbon dioxide both
decrease hb affinity for oxygen
77
when proteins denature the structures is lost but
primary structure remains in intact