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Biochem II part 2 terms > terms > Flashcards

terms Flashcards

1
Q

This amino acid has an aromatic ring and is neutral at pH 7 however when it pH 5 it becomes active

A

His (histidine)

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2
Q

This little guy is non-polar and is very flexible because it has no side chain

A

Gly (glycine)

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3
Q

This amino acid is charged and has a carboxylate group on it

A

Asp (aspartate)

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4
Q

this amino acid 3 carbons in its side chained followed by nitrogen

A

Lys (lysine)

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5
Q

This amino acid is able to form disulfide bonds

A

Cys (cysteine)

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6
Q

This amino acid has an aromatic ring with a hydroxyl group on the end

A

Tyr (tyrosine)

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7
Q

This amino has a small side chain, polar and a hydroxyl group on the end

A

Ser (serine)

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8
Q

this amino acid has a cyclic side chain and is very rigid

A

Pro (proline)

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9
Q

The sequence of amino acid side chains is determined by DNA sequence of gene

A

primary structure

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10
Q

This is the hydrogen bonding of the peptide backbone and not directly dependent on sidecahins

A

secondary structure

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11
Q

this is the 3-dimensional packing of a whole protein chain

A

tertiary structure

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12
Q

this is the interaction between global domains such as actin & myosin, collagen, hemoglobin (association between multiple protein molecules)

A

quaternary structure

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13
Q

this is a protein that is more or less spherical in shape and has less surface area to volume ratio

A

globular domain

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14
Q

This is a protein that is very elongated and usually has some structural function

A

fibrous protein

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15
Q

connects i, i+4 amide groups and is has self-contained hydrogen bonding. binds carbon (i) and another carbon 4 away (i+4`)

A

alpha helix

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16
Q

this are things that allows the amino acid to rotate is two different places and they are known as.

A

phi/psi angles

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17
Q

this is important in understanding protein structure and lead to steric hinderance

A

torsion angles

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18
Q

if molecules are brought to close together and want to repel this is known as

A

steric hindrance

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19
Q

_______ can either lead to the polypeptide being in parallel form or antiparraller

A

beta sheet

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20
Q

without the _____ the enzyme may be unable to function like thiamine is a _____ for pyruvate dehydrogenase

A

cofactor

21
Q

_____ aka iron

A

heme

22
Q

this protein is composed of two alpha-helices wrapped around each other and they can be help together by disulfide linkages to become long stiff fibers

A

keratin

23
Q

A _____ ______l is a structural motif in proteins in which 2-7 alpha-helices are coiled together like the strands of a rope

A

coiled coil

24
Q

this is essentially a triple helix made from gly-pro-(anything else) and results in a very stiff, strong and is non-strecthy. Therefore it is good for bones and tendons

A

collagen

25
Q

______ is composed of three polypeptides that are interwound such as DNA

A

triple helix

26
Q

This occurs when molecules are afraid of water and wanter to be in the middle of the protein away from the water

A

hydrophobic effect

27
Q

When a protein becomes unfolded this is referred to as

A

denaturation

28
Q

this is a chaperone that helps unfold misfolded proteins

A

GroEL/GroES

29
Q

sigmoid curve is the hallmark and when one thing binds more things want to bind. For example when people realize alex is taken all of the sudden they want to join

A

positive cooperativity

30
Q

the binding sites become weaker after the initial thing binds and makes response to changes in substrate concentration more gradual, allowing for a broader dynamic range

A

negative cooperativity

31
Q

this is an allosteric effector that binds to hemoglobin lower the binding affinity for oxygens and going towards the T state

A

2,3-BPG

32
Q

This molecule is a competitive inhibitor with oxygen and can be removed from hemoglobin if p___ drops again

A

carbon monoxide

____=CO

33
Q

something that fights with the correct molecule to bind in the active site is known as???

A

competitive inhibitor

34
Q

Something that binds away from the active site and cause the molecule to become less active

A

allosteric inhibitor

35
Q

Something that binds away from the active site and cause the molecule to become more active

A

allosteric activator

36
Q

multiple forms of proteins-

multiple form os enzymes

A

isoform Ex Hb and HbF

isozyme

37
Q

Helix rest in major groove of DNA and protein fold up around the ZN++ ion. Pretty much the smallest protein

A

zinc finger protein

38
Q

reconition helix nestles into major groove and contacts bases (reads sequence). Stabilization helix sits behind it, and contacts the DNA backbone.

A

helix-turn-helix proteins

39
Q

????

A

examples

40
Q

very similar to chymotrypsin, essentially they are divergent

A

trypsin

41
Q

this is the precursor to trypsin

A

trypsinogen

42
Q

_____ has ser, asp and his in the active site and responsible for catalysis

A

chymotrypsin

43
Q

this is the precursor to chymotrypsin

A

chymotrypsinogen

44
Q

________ is an enzyme whose zymogen (pepsinogen) is released by the chief cells in the stomach and that degrades food proteins into peptides.

A

pepsin

45
Q

________ is a non-specific protease (a protein-digesting enzyme) initially obtained from Bacillus subtilis

A

subtilisin

46
Q

_________ is an enzyme produced by cells of the duodenum and involved in human and animal digestion

A

enteropeptidase

47
Q

The _____ ______ are a family of enzymes that ydrolyzecertain peptide bonds in other proteins.

A

serine protease

48
Q

A _____ ______ is a group of three amino acids that are found in the active sites of some proteases involved in catalysis

A

catalytic triad

49
Q

An _____ _____ is a pocket in the structure of an enzyme which stabilizes a deprotonated oxygen or alkoxide, often by placing it close to positively charged residues. In our case it stables the tertiary structure of the serine protease mechanism

A

oxyanion hole

Biochem II part 2 terms (1 decks)

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