Proteins Flashcards
(92 cards)
1
Q
A _____ bond is specific to the amide bond in proteins
A
peptide
2
Q
A peptide bond is between the ____ group of one amino acid and the ____ group of another amino acid
A
carboxyl (COO-), amino (NH3+)
3
Q
____ is released during a peptide/amide bond formation
A
water
4
Q
The byproduct of a peptide bond formation is a _______
A
dipeptide
5
Q
A dipeptide has a ___ end and ____ end
A
N-terminal, C-terminal
6
Q
The backbone of a dipeptide is repeated _________ units with R side chains
A
N-C alpha-C
7
Q
The atoms around a peptide bond (CO-NH) are _______
A
coplanar (2D)
8
Q
_____ is the enzyme that breaks down RNA molecules
A
ribonuclease
9
Q
The R side chain of the protein is ______
A
hydrophobic
10
Q
The inside of a protein is ______
A
hydrophillic
11
Q
______ is a protein that attacks bacterial cell walls
A
lysosine
12
Q
Every copy of the same protein follows ____ folding patterns
A
the same
13
Q
Proteins have ____ numbers of chains and disulfide bonds
A
varied
14
Q
The most abundant protein in humans (25-30% of all proteins) is _____
A
collagen
15
Q
Collagen is ____ shaped
A
fibrous
16
Q
Collagen is 1/3 ____ and is rich in _____
A
glycine, proline
17
Q
A phylogenetic tree compares amino acid sequences of the protein ________
A
cytochrome C
18
Q
On a phylogenetic tree, amino acid _____ are on the branches
A
changes
19
Q
_____ proteins require something bound to them to activate
A
conjugated
20
Q
The binding of nonprotein groups affect protein _____
A
folding
21
Q
Glyco means ____
A
carbohydrate
22
Q
Lipo means _____
A
lipid
23
Q
Nucleo means _____
A
DNA or RNA
24
Q
Metallo means _____
A
metal ion
25
Ribonuclease and trypson are examples of what protein function?
enzymes (catalyst)
26
Insulin, trans factor NF-1 are examples of what protein function?
regulatory
27
Hemoglobin and glucose transporter and examples of what protein function?
transport
28
casein and ovalbumin are examples of what protein function?
storage
29
casein and ovalbumin are examples of what protein function?
storage
30
actin, myosin, and tubulin are examples of what protein function?
contractile/motile
31
Collagen and a-keratin are examples of what protein function?
structural
32
Immunoglobulins and fibrinogen are examples of what protein function?
protective
33
Antifreeze and glue proteins are examples of what protein function?
exotic
34
_____ separates ions on the basis of charge
chromatography
35
____ ____ ______ separates ions on the basis of size
size exclusion chromatography
36
_____ _______ separates ions on the basis of affinity (specific binding to small molecules)
affinity chromatography
37
_____ is the movement in an electric field
electrphoresis
38
______ separates ions on the basis of molecular weight
SDS-PAGE (SDS-polyacrylamide gel electrophoresis)
39
____ _____ separates ions on the basis of isoelectric point (pl)
isoelectric focusing
40
pl is a measure of the ____ of the side chain
pH
41
____ ___ ____ ______ separates ions on the basis of isoelectric point and molecular weight (added)
two dimensional gel electrophoresis
42
___ protein shape is linear molecules that serve structural roles
fibrous
43
____ protein shape is a cluster of hydrophobic amino acid insides and hydrophilic amino acid outsides
globular
44
_____ protein shape interacts with membrane lipids and has hydrophobic amino acids on the outside
membrane
45
collagen is an example of what protein shape?
fibrous
46
myoglobin is an example of what protein shape?
globular
47
bacteriorhodopsin is an example of what protein shape?
membrane
48
What is the first level of protein structure?
primary
49
What is the second level of protein structure?
secondary
50
What is the third level of protein structure?
tertiary
51
What is the fourth level of protein structure?
quartenary
52
_____ structure is the amino acid sequence of a protein
primary
53
_____ structure is the short range structure in a protein, either alpha helix or beta strand
secondary
54
____ structure is the folding of a polypeptide into it's 3D shape
tertiary
55
_____ structure is the numbers and kinds of polypeptide subunits in a protein
quaternary
56
_____ structure forms the polypeptide backbone
secondary
57
______ structure is the spatial arrangement of polypeptide chains
quaternary
58
Ribonuclease is roughly ____ a.a. long
124
59
_____ ____/______ are amino acid sequences used repeatedly in a single protein or that are found in different proteins
protein domains/modules
60
Protein domains/modules are typically ____ to ____ amino acids long
40-100
61
Protein domains do/do not have the same function in different proteins
do not
62
What type of protein domain is unusual and less common?
different proteins
63
Domains in _____ occur from faulty DNA replication
the same protein
64
Domains in ____ occur after the insertion of a copy of a DNA segment into another gene
different proteins
65
Some domains are ____ and their function is unknown
neutral
66
Domains ____ over time and become unrecognizable to the original
mutate
67
A newly synthesized protein first forms segments of ____ _____
secondary structure (alpha helix, beta sheets)
68
____ bonding occurs along segments of polypeptides and between segments
H
69
Secondary structure of polypeptides arrange into a ______ shape by hydrophobic interactions
globular
70
Secondary structure of polypeptides arrange into a globular shape by _______
hydrophobic interactions
71
Hydrophobic R side chains want to cluster where?
away from water, middle of protein
72
Can secondary structure change during the generation of the tertiary structure?
yes
73
Protein folding may need to assistance of ____ _____
molecular chaperones
74
What is the role of molecular chaperones?
proteins in cell, bind to the new protein and bring parts together to obtain proper 3D folded
75
Do all proteins need molecular chaperones?
no
76
___ ____ are misfolded, insoluble, and aggregated proteins in brain cells
amyloid deposits
77
What protein is misfolded in Alzheimer's disease?
amyloid-b
78
What protein is misfolded in Parkinson's disease?
a-synuclein
79
____ _____ are protein subunits that combine to form multi-subunit complexes
Quaternary structures
80
Proteins can have either ____ subunits or _____ types of protein chains
identical, different
81
The ______ produces quaternary structure are the same as those used for tertiary structure
forces
82
What 4 things play a role in quaternary structure production?
hydrophobic interactions, hydrogen bonding, ionic interactions, disulfide bonds
83
Quaternary structure allows for _____ _____ between protein subunits
cooperative behavior
84
In hemoglobin, there are ____ protein subunits
4
85
How does hemoglobin exhibit cooperative behavior?
The binding of the first O2 molecule makes it easier for the other 3 O2 molecules to bind to the protein subunits
86
Hemoglobin aides in what physiological function?
rapid release of O2 into lungs
87
What are the two types of quaternary structure?
fixed number, open
88
What are microtubules?
long, hollow tubes
89
Where are microtubules found?
cytoskeleton (cell structure), mitotic spindles (cell division process)
90
Tubulin dimers _____ to form microtubules
polymerize
91
Microtubules are dynamic and can easily ______
increase or decrease in length
92
Microtubules have ____ quaternary structure
open
