Proteins and Amino Acid Flashcards

1
Q

What level of protein structure is associated with the sequence of amino acids?

A

primary

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2
Q

What are monomers

A

amino acids (there are 20 diff ones) that are the SAME 20 in all living things

(molecule that can be bonded to form a polymer), amino acids (monomer) can be bonded to form protein (polymer)

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3
Q

What are amino acids made up of

A

75%= dry body mass

95%= muscle (and heart)

100%= of hormones, neurotransmitters, and neutropeptides

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4
Q

Polymer: Polypeptide chain

A
  • chain of amino acids (linear), they’ll interact in a polar and non polar fashion
  • polypeptide chains will form shapes (3D structure/conformation=protein, important bc form follows function)
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5
Q

Proteins interact in our body to do?

A

form hair, mucus, cartilage, enzymes, etc.

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6
Q

Importance of variable group in an amino acid

A
  • can put any of the 20 different amino acids there, made up of or less than
  • gives the amino acids their characteristics
  • overall polar molecule
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7
Q

Same, molecule, different arrangement (left and right hand mirror images) is called a ?

A

an optical isomer

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8
Q

are amino acids acidic or base?

A

both acidic or basic, R group will thus, determine the behaviour (depending on whether or not an acid/base is added as the R group)

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9
Q

Same basic structure, different R groups

A

drive the shape of the molecule

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10
Q

changes in protein structure causes

A

disease, syndrome, etc.

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11
Q

small changes in proteins

A

= Changes in phenotype

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12
Q

Amino Acids Overview…
How many are essential?
Types?
How they’re brought in?

A

8-10 are essential, our bodies can’t make them

(Phenylaline, valine, threonnie, tryptophan, methionine, leucine, isoleucine, lysine, and histidine, sometimes arginine)

  • must be brought in via diets (incomplete/complete sources of proteins)
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13
Q

what are most amino acids

A

most are precursors to neurotransmitters, or hold proteins together

(building block)

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14
Q

what is a peptide

A

2+ amino acids joined by a peptide bond

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15
Q

what is a peptide chain/bond

A

holds proteins together, like insulin

  • have a linear structure: n and c terminus
  • order and sequence determine structure
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16
Q

what is the order of a peptide chain driven by?

A

genes

17
Q

what do amino acids drive

A

interactions between amino acids and r-groups

18
Q

protein structure

A

1) primary structure: sequence, order of amino acids

2) secondary structure: hydrogen bonds, a-helix, and b-pleated sheets

3) tertiary structure: disulphide bridges and polar vs non polar

4) quarternary structure
(different subunits or pieces) **NOT ALL PROTEINS GET HERE

19
Q

proteins will have

A

a hydrophobic core, this is why they want to be in the middle

20
Q

what will the order of amino acids influence?

A

the shape of the molecule, for example, the presence of cystine curls hair

21
Q

Protein Folding:

  • electrostatics refers to
A

opposites attract, like charges repel

22
Q

cystine buddies form

A

dusulphide bridges

23
Q

how is the shape important

A

form follows function, determines how the protein behaves

24
Q

what happens to a protein if we add heat or acid

A
  • changing the intermolecular attractions of R-group
  • ## changing the 3D shape/structure of proteins
  • called denaturation of proteins (disrupts hydrogen bonds, ionic bonds, disulphide bridges: temp, pH, salinity)

For ex. can’t uncool an egg

25
Q

what is denaturation

A

the breaking of the any linkages, or bonds, (ex. hydrogen bonds)

26
Q

what are polypeptides polymers of

A

amino acids

27
Q

how are amino acids also joined

A

via a dehydration synthesis method of -COOH and -NH2 that forms water and results in a dipeptide

28
Q

all of the protein structure steps occur in which organelle?

A

rough e.r. because of the ribosomes, and chaperone proteins

the rough e.r. ensures the proteins get into the desired shape

29
Q

why do alpha helixes occur

A

hydrogen bonding

30
Q
A