Chapter 4 Flashcards

(40 cards)

1
Q

structural proteins

A

provides cell with shape and structure

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2
Q

enzymes

A

catalyze covalent bond breakage or formation

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3
Q

transport protein

A

carries other molecules or ions

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4
Q

motor protein

A

generates movement in cell and tissue

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5
Q

storage protein

A

stores small molecules or ions

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6
Q

signal protein

A

carries signal from cell to cell

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7
Q

receptor protein

A

detects signals and transmits them to cells response machinery

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8
Q

gene regulatory protein

A

binds to DNA to switch genes on or off

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9
Q

what bonds link amino acids?

A

peptide bonds

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10
Q

what is protein made of?

A

amino acids linked together into polypeptide chain

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11
Q

what 3 noncovalent bonds help proteins fold?

A

hydrogen bonds, electrostatic attractions, van der waals attraction

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12
Q

what interaction is most important for protein folding?

A

hydrophobic interaction

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13
Q

what causes proteins to denature?

A

urea. denature proteins unfold to natural shape

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14
Q

how are prion diseases caused?

A

by rare proteins whose misfolding is infectious.

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15
Q

what is a common folding pattern?

A

alpha helix

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16
Q

alpha helix

A

the amino group of every peptide bond is h-bonded to carboxyl group of neighboring peptide bond located 4 amino acids away.

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17
Q

what is another common folding pattern of proteins?

18
Q

beta sheet

A

individual strands in sheet held together by h-bonding between peptide bonds in different strands.

19
Q

what are the two varieties of beta sheets?

A

parallel and Antiparallel

20
Q

what is comprised of a family of proteolytic enzymes?

A

serine proteases

21
Q

many protein molecules contain _____ of a single protein subunit.

A

multiple copies

22
Q

proteins can assemble into what?

A

complex structures. dimer, helix, and ring

23
Q

what is an actin filament composed of?

A

identical protein subunits

24
Q

single protein subunits can pack to form what?

A

a filament, tube, or a spherical shell

25
what is a collagen?
a triple helix formed by 3 protein chains to wrap around one another
26
what do disulfide bonds do?
help stabilize a favorable protein confomation
27
folding of a polypeptide chain creates what on protein surface?
cavity
28
binding sites allow proteins to do what?
interact with specific ligands.
29
what is an antibody?
y-shaped and has two identical binding sites for its antigen.
30
what is feedback inhibition?
regulates the flow through biosynthetic pathways
31
what does feedback inhibition do?
triggers a conformational change
32
what does an increase in ligand (ADP) concentration do?
activates the enzymatic reaction for oxidation of sugars
33
what conformation can ADP bind to? why?
closed. lowers energy of closed conformation, locking enzymes in the active site
34
What is a common mean of regulating protein activity?
protein phosphorylation
35
what does GTP-binding proteins from?
molecular switches.
36
an allosteric motor protein driven by ATP hydrolysis moves in what direction? why?
one direction. repeated cycles of conformation changes, the proteins moves continuously
37
how is protein behavior controlled?
modification of a protein at multiple sites produce a regulatory code that controls the PB
38
how can the structure of protein be determined?
x-ray crystallography
39
cells in culture display properties that reflect what?
their origin
40
what is affinity chromatography used for?
to isolate the binding partners of a protein of interest