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Pass The Dental Boards > Proteins > Flashcards

Proteins Flashcards

1
Q

What is another name for a peptide bond?

A

amide bond

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2
Q

What is a usefull function of the negative charge of proteins?

A

It can buffer a solution

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3
Q

What direction does a primary structure go?

A

From N terminus to C terminus

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4
Q

how is a secondary structure stabilized?

A

Via hydrogen bonds between the R groups

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5
Q

What is a beta turn?

A

a type of secondary structure that is composed of PROLINE

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6
Q

What does proline do in a tertiary structure?

A

It contributes to the bends and turns.

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7
Q

What helps a tertiary structure remain stable?

A

cysteine bonds (disulfur bonds are cysteine to cysteine sulfur bonds)

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8
Q

What are two key examples of quaternary proteins?

A

hemoglobin and antibodies

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9
Q

What type of bond is a peptide bond?

A

covalent

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10
Q

What does denaturing protein bonds do?

A

breaks all of the bonds except the covalent peptide and disulfur bonds.

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11
Q

What enzyme can break peptide bonds?

A

protease

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12
Q

What is the best method of determining the 3D structure of a protein?

A

Xray diffraction

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13
Q

What does electrophoresis do?

A

separates proteins based on size and charge

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14
Q

What are the 5 groups of amino acids?

A
  1. non-polar, aliphatic R groups
  2. Aromatic R groups
  3. Polar, uncharged R groups
  4. Positively charged R groups
  5. Negatively charged R groups
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15
Q

What is the only amino acid that is not Chiral?

A

glycine

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16
Q

Which amino acids are aromatics?

A

Its pheny when you tryp on a tyre

phenylalanine
tryptophan
tyrosine

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17
Q

What are the positively charged amino acids?

A

Basically (+) the HISTory of ARGINtina is a LYe

histadine
arginine
lysine

18
Q

What are the negatively charged amino acids?

A

Ass and gluts are negative

aspartate
glutamate

19
Q

Which amino acids are exclusively ketogenic?

A

leucine and lysine (L and L)

20
Q

Which amino acids are both glucogenic and ketogenic?

A

PhITTT (they are so fit that they can do both!)

phenylalanine
isoleucine
tyrosine
threonine
tryptophan
21
Q

What is an amino acid called if its broken down for energy?

A

alpha keto acids

22
Q

Which configuration are amino acids in? L or D?

A

ALL of us want to be a DDS

Amino acids - L
Sugars - D

23
Q

Which amino acids are made from pyruvate?

A

LIVA pye

Leucine, isoleucine, valine, alanine

24
Q

What is the R group for alanine?

A

methyl group

25
Q

What protein is found in collagen and elastin?

A

glycine (about 33% of them is glycine)

26
Q

What is the amino acid that is the simplest structure with a hydrogen for its R group?

A

glycine

27
Q

What is glycine used to make?

A

creatine, purines, porphyrin

Glycine CREATES PURE PORES

*its also used to make glycocholic acid ( a bile salt)

28
Q

What amino acid substitution creates sickle cell anemia?

A

valine is substituted for glutamate

29
Q

What is the amino acid in a start codon?

A

methionine (AUG)

30
Q

What amino acid is only essential in people with phenylketonuria?

A

phenylalanine, which makes tyrosine

31
Q

What are the two source of the urea cycle?

A

aspartate and carbamoyl phosphate

32
Q

What are hydroxyproline and hydroxylysine?

A

Non-standard amino acids found in collagen.

33
Q

What is lysyl hydroxylase?

A

an enzyme that adds the OH group to proline and lysine to make hydroxyproline and hydroxylysine.

34
Q

What does lysyl hydroxylase require to work?

A

Vitamin C

35
Q

What is the most abundant protein in blood serum?

A

albumin

36
Q

What is the most abundant protein in the body by weight?

A

collagen

37
Q

What form of collagen is in the cytosol of a fibroblast?

A

procollagen

38
Q

How does elastin differ from collagen other than its stretchiness?

A

elastin has lysine crosslinks

collagen has disulfide crosslinks

39
Q

What does transferrin do?

A

transports Iron

40
Q

What is cytochrome?

A

a protein that has a metal core, usually of iron and acts to transport electrons like in the ETC

Pass The Dental Boards (4 decks)

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