Proteins/protein structure 1 Flashcards

1
Q

four levels of protein structure

A

primary
secondary
tertiary
quaternary

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2
Q

protein classification by shape

A

globular vs fibrous

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3
Q

protein classification by composition

A

simple vs conjugated

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4
Q

contain only amino acids

A

simple proteins

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5
Q

contain protein and ‘non protein’ components

A

conjugated proteins

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6
Q

the specific amino acid sequence of a protein

A

primary structure

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7
Q

similar sequence and arose from the same ancestor gene, and carry out similar fuctions

A

homologous proteins

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8
Q

sickle cell anemia is caused by a substitution of _____ for a ____

A

valine for a glutamate

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9
Q

polypeptide bond between nitrogen on amino group and alpha carbon

A

phi bond

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10
Q

polypeptide bond between alpha carbon and carboxyl carbon

A

psi bond

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11
Q

polypeptide bond between carboxyl carbon and nitrogen of amino group

A

omega bond

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12
Q

structures stabilized by hydrogen bonding between carbonyl and the N-H groups of polypeptide’s backbone

A

secondary structure

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13
Q

two most common secondary structures

A

alpha helix

beta pleated sheet

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14
Q

a rigid, rod-like structure formed by a helical turn

A

alpha helix

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15
Q

alpha helix are stabilized by hydrogen bonding between N-H and a carbonyl group ____

A

four amino acids away

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16
Q

two amino acids that do foster alpha helix

A

glycine

proline

17
Q

why doesn’t glycine form alpha helix

A

its to small and flexible

18
Q

why doesn’t proline form alpha helix

A

too rigid, lacks a N-H group for hydrogen bonding

19
Q

which are more abundant in nature left or right handed secondary structures

A

right handed secondary structures

20
Q

three different types of right handed alpha helices

A

alpha helix
3-10 helix
pi helix

21
Q

form when two or more polypeptide chain segments line up, side by side

A

beta pleated sheets

22
Q

two types of beta pleated sheets

A

parallel

antiparallel

23
Q

which type of beta sheet is less stable

A

parallel sheets

24
Q

many proteins have supersecondary structures with patterns of alpha helix and beta sheets

A

motifs

25
Q

refers to unique three dimensional structures formed by globular proteins

A

tertiary structure

26
Q

four main chemical interactions help stabilize tertiary structure

A

hydrophobic interactions
ionic interactions
hydrogen bonds
covalent bonds

27
Q

hydrophobic R groups are brought together as they exclude water or are excluded fro water

A

hydrophobic interactions

28
Q

occurs between R goups of amino acids

A

hydrogen bonding

29
Q

includes disulfide bridges

A

covalent bonds

30
Q

occurs especially between oppositely charged groups

A

ionic interactions

31
Q

structurally independent segments that have specific functions

A

domains

32
Q

core structural element of a domain is

A

fold

33
Q

proteins that consist of repeated domains

A

mosaic or modular proteins

34
Q

level of structure achieved when two or more folded polypeptides in tertiary structure associate to form a functional protein

A

quaternary structure

35
Q

individual polypeptides in quaternary structure are called

A

subunits

36
Q

three reasons for common occurrence of multiunit proteins

A
  1. synthesis of subunits is more efficient
  2. worn out subunits can be replaced more effectively
  3. biological function requires interaction of subunits
37
Q

polypeptide subunits are held together by

A

linkages

38
Q

covalent cross links in collagen are initiated by

A

lysyl oxidase

39
Q

some proteins are partially or completely unstructured

A

unstructured proteins