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Bio 302 > Chapter 4 > Flashcards

Chapter 4 Flashcards

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Biology 101 flashcards
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?

A

beta sheets

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
Q

what is a collagen?

A

a triple helix formed by 3 protein chains to wrap around one another

26
Q

what do disulfide bonds do?

A

help stabilize a favorable protein confomation

27
Q

folding of a polypeptide chain creates what on protein surface?

A

cavity

28
Q

binding sites allow proteins to do what?

A

interact with specific ligands.

29
Q

what is an antibody?

A

y-shaped and has two identical binding sites for its antigen.

30
Q

what is feedback inhibition?

A

regulates the flow through biosynthetic pathways

31
Q

what does feedback inhibition do?

A

triggers a conformational change

32
Q

what does an increase in ligand (ADP) concentration do?

A

activates the enzymatic reaction for oxidation of sugars

33
Q

what conformation can ADP bind to? why?

A

closed. lowers energy of closed conformation, locking enzymes in the active site

34
Q

What is a common mean of regulating protein activity?

A

protein phosphorylation

35
Q

what does GTP-binding proteins from?

A

molecular switches.

36
Q

an allosteric motor protein driven by ATP hydrolysis moves in what direction? why?

A

one direction. repeated cycles of conformation changes, the proteins moves continuously

37
Q

how is protein behavior controlled?

A

modification of a protein at multiple sites produce a regulatory code that controls the PB

38
Q

how can the structure of protein be determined?

A

x-ray crystallography

39
Q

cells in culture display properties that reflect what?

A

their origin

40
Q

what is affinity chromatography used for?

A

to isolate the binding partners of a protein of interest

Bio 302 (7 decks)

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