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BIOCHEM > PROTEINS > Flashcards

PROTEINS Flashcards

1
Q

polymers unbranched chains of amino acids present

A

Protein

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2
Q

% of protein in cell’s mass
% of nitrogen content

A

15%
15.4%

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3
Q

composition of protein

A

carbon, hydrogen, nitrogen, oxygen & sulfur

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4
Q

None of standard amino acids are chiral : T/F

A

True

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5
Q

has 20 alpha amcid; found in proteins

A

Standard amino acid

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6
Q

nonpolar amino acids are:

A

hydrophobic & found in interior of protein

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7
Q

polar amino acids are:

A

hydrophilic

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8
Q

3 polar amino acids

A

neutral
acidic
basic

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9
Q

has carboxyl group part of side chains ; 2 amcid

A

acidic

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10
Q

has 1 amino group part of side chain ; 3 amcid

A

basic

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11
Q

has 6 amino acids

A

neutral

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12
Q

3 letter naming amcid

A

Nomenclature

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13
Q

1 letter nomenclature

A

computing amcid sequence

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14
Q

Chirality of amcid

A

4 diff groups attach to alpha carbon atom except glycine (r group is hydrogen)

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15
Q

amino acids in nature/proteins are:

A

L-isomers

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16
Q

give up protons ; - charged species

A

Carboxyl groups

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17
Q

accept protons ; + changed species

A

Amino groups

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18
Q

ph where amcid exist in zwitter form

A

Isoelectric point

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19
Q

3 types of peptide

A

Dipeptide
Oligopeptide
Polypeptide

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20
Q

covalent bonds between amcids

A

Peptide bonds

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21
Q

peptide w same amcid but present in diff order

A

Isometric peptide

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22
Q

small peptide hormones

A

Oxytocin & vasopressin

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23
Q

Regulate uterin contractions

A

Oxytocin

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24
Q

regulate secretion of water

A

Vasopressin

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25
pentapeptide neurotransmitters by the brain ; bind receptor sites
Enkephalins
26
tripeptide in high levels in most cells
Glutathione
27
has unusual structure feature; regulates oxidation; protects cellular contents from agents
Glutathione
28
Structure of gluta
Glu bonded to cys through side chain carboxyl group
29
protein classification:
Simple & conjugated protein
30
1/more amcid & POLY CHAIN (prostetic groups present) (PROTEIN)
Conjugated
31
protein w carbohydrate group
glycoprotein
32
structures of protein:
Primary, secondary, tertiary & quarternary
33
order where amcid are linked together in protein
Primary structure
34
he sequenced primary structure of first protein (insulin)
Frederick Sanger
35
planar, has rigidity
Peptide linkages
36
arrangement adopted by backbone portion of a protein
Secondary protein structure
37
structure (coiled spring) maintained by hydrogen bonds ; right handed
Alpha helix structure
38
2 fully extended protein segments in mol ; arizes from zigzag pattern
Beta pleated sheets
39
3 dimentional shape of protein l widely separated
Tertiary structure
40
occur between acids w polar r groups
Hydrogen bond
41
2 nonpolar chains close to each other
Hydrophobic attractions
42
organization of peptide units in multimeric protein
Quarternary structure
43
results in regeneration of amino & carboxyl
Protein hydrolysis
44
absorbed in blood stream to new proteins
free amino acid
45
disorganizations of proteins 3d shape
Protein denaturation
46
Precipitation of denaturated protein
Coagulation
47
protein mol w peptide chain into spherical shape ; water soluble
Globular proteins
47
proteins w elongated shapes
fibrous proteins
48
most abundant protein in humans (30%)
Collagen
49
structure of collagen
triple helix (maintained by glycine & proline)
50
oxygen carrier mol in blood ; tetramer
Hemoglobins
51
oxygen storage molecule in muscles ; higher affinity than hemo
Myoglobins
51
CLASSIFICATION FUNCTIONOF PROTEINS
Catalyst Defense Transport Messenger Contractile Structural Transmembrane Nutrient Buffer Fluid balance Storage Regulatory
51
Defense Function ex:
immunoglobulins/antibodies
52
Messenger function ex
insulin, glucagon
53
(function) Form of movement
Contractile
54
ex of Contractile
actin, myosin; human repro
55
Structural ex
Collagen, cartilage, keratin
56
transmembrane (function)
control movement of small mol & ions
57
Storage exampls
Feritin & Myoglobin
58
(function) exterior surface of cell membranes ; enzymes
Regulatory
59
(function) important from embryo to infant
Nutrient
60
Nutrient examples (function)
Casein ; Ovalbumin (eggwhite)
61
maintains acid balance (function)
Buffer
62
has carbohy derivatives addition to amcid
Glycoproteins
63
Structual feature of Collagen
4 hydroxyproline & 5 hydroxylsine
64
protective response to invasion of microorganism
Immunoglobulins
65
foreign substance ; bacteria/virus
Antigen
66
biochem mol counteracts w antigen
Antibody
67
suspends lipid & transports them through blood stream
Lipoproteins
68
transport system ; spherical feature ; central core of lipid material
Plasma lipoproteins
69
Classes of Plasm Lipoproteins
Chylomicrons Very low density Lipoproteins Low density lipoproteins High denisty lipoproteins
69
transport dietary glycerols
Chylomicrons
70
Transport triacyl synthesized
Very low density lipoproteins
71
Transport cholesterol synthesized
Low density lipoproteins
72
collect excess cholesterol from body tissues
High density Lipoprotein
73
amcid producing disulfied bonds
cysteine-cysteine
74
polypeptide chains in beta pleated sheet conformation are held by
hydrogen bonding
75
some simple proteins are conjulated proteins: T/F
TRUE
76
standard amino acid with out alpha carbon
glycine

BIOCHEM (8 decks)

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