BIOCHEM: PROTEIN Flashcards

1
Q
  • Naturally occurring, unbranched polymer
  • Monomers: AMINO ACIDS
A

Proteins

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2
Q
  • Building blocks for proteins
  • Organic compound that contains both –NH2 and –COOH
A

Amino Acids

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3
Q
  • posttranslational
    modification of
    proteins
A

SERINE

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4
Q
  • active part of
    many enzymes
  • synthesis of CoA
A

Cysteine

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5
Q

posttranslational
modification of
proteins

A

Threonine

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6
Q

posttranslational
modification of
proteins

A

Asparagine

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7
Q
  • Nitrogen carrier
A

Glutamine

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8
Q

Precursor of:
Phenylalanine, Tyrosine, Levodopa

A

Tyrosine

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9
Q
  • participates in many
    metabolic pathways
A

Aspartic Acid

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10
Q
  • ionic form is an
    excitatory NTA - precursor of GABA
A

Glutamic Acid

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11
Q
  • precursor of
    Histamine
A

Histidine

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12
Q
  • precursor of
    Carnitine
A

Lysine

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13
Q

precursor of
Creatinine &
Urea

A

Arginine

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14
Q

standard amino acid needed by the body that must be obtained from
the diet because the body cannot synthesize them in adequate
amounts

A

Essential Amino Acids

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15
Q

–contains ALL of the essential amino
acids in the same relative amounts that the body needs them

A

COMPLETE dietary protein

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16
Q

–does not contain adequate amounts
OR does not contain all of the essential amino acids

A

INCOMPLETE dietary protein

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17
Q

essential amino acid that is missing or
present in inadequate amounts In an incomplete dietary protein

A

LIMITING amino acid

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18
Q

–COOH at the top
–R group at the bottom
–NH2 positioned horizontally

A

Fischer Projection

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19
Q

T or F
AAs are charged species both in solid state and in solution

A

true

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20
Q
  • pH at which the AA exists primarily in zwitterion form (>99%)
A

ISOELECTRIC POINT

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21
Q

Unbranched chain of
covalently-linked AAs

22
Q

amide bond that covalently links the –COOH
group of one AA and –NH2 group of another AA

A

PEPTIDE BONDS

23
Q

T or F
Peptide chains have directionality because it has 2 different ends

24
Q

The C-terminal AA residue keeps its full AA name.

A

Peptide Nomenclature

25
Peptides containing the same AAs but in different order
Isomeric Peptides
26
Nonapeptide with 6 AAs in a loop held by a disulfide bond
OXYTOCIN
27
Nonapeptide with 6 AAs in a loop held by a disulfide bond
VASOPRESSIN (ADH)
28
* Pentapeptide * Met-enkephalin: Tyr–Gly– Gly–Phe–Met
ENKEPHALINS
29
- binds receptors in the brain to reduce pain
Neurotransmitter
30
- Protects cellular contents from reactive oxygen species
Antioxidant
31
protein – only one peptide chain
Monomeric protein
32
more than one peptide chain (subunits)
Multimeric protein
33
only AA residues are present
Simple protein
34
– one or more peptide chains + one or more
Conjugated protein
35
2 fully extended protein chain segments in the same or different molecules are held together by hydrogen bonds
BETA PLEATED SHEET
36
– protein secondary structure that is neither an ⍺ helix nor a β pleated sheet
Unstructured segment
37
Overall 3D shape of a protein due to the interactions between amino acid side chains (R groups)
Tertiary Structure
38
* Highest level of protein organization * Found only on multimeric proteins
Quaternary Structure
39
Occurs when a protein or small peptide in a solution of strong acid or base is heated
Hydrolysis
40
– all peptide bonds are broken, freeing up all AAs
Complete hydrolysis
41
– some, but not all peptide bonds are broken, producing a mixture of free Aas and small peptides
Partial hydrolysis
42
– enzyme-catalyzed hydrolysis of ingested proteins
Protein digestion
43
Partial or complete disorganization of a protein’s characteristic 3D shape due to disruption of its secondary, tertiary, or quaternary structural interactions
Denaturation
44
* Protective coating for organism * Found in hair, fingernails, toenails, wool, feathers, claws
ALPHA KERATIN
45
* Most abundant protein * Found in skin, bones, tendons, ligaments, blood vessels
COLLAGEN
46
* Stores O2 in the muscles * Monomer that contains a heme group
MYOGLOBIN
47
* Transports O2 from the lungs to the tissue * Tetramer with each subunit containing a heme group
HEMOGLOBIN
48
Conjugated protein produced by an organism as a protective response to specific foreign substances
Immunoglobulins
49
Conjugated protein used to suspend lipids and transport them through the bloodstream
Lipoproteins
50