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?

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
what is denaturation
the breaking of the any linkages, or bonds, (ex. hydrogen bonds)
26
what are polypeptides polymers of
amino acids
27
how are amino acids also joined
via a dehydration synthesis method of -COOH and -NH2 that forms water and results in a dipeptide
28
all of the protein structure steps occur in which organelle?
rough e.r. because of the ribosomes, and chaperone proteins the rough e.r. ensures the proteins get into the desired shape
29
why do alpha helixes occur
hydrogen bonding
30