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2ND YEAR MIDTERMS > BIOCHEM: PROTEIN > Flashcards

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

A

Peptides

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

A

True

24
Q

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

A

Peptide Nomenclature

25
Q

Peptides containing the same AAs but in different order

A

Isomeric Peptides

26
Q

Nonapeptide with 6 AAs in a
loop held by a disulfide bond

A

OXYTOCIN

27
Q

Nonapeptide with 6 AAs in a
loop held by a disulfide bond

A

VASOPRESSIN (ADH)

28
Q
  • Pentapeptide
  • Met-enkephalin: Tyr–Gly–
    Gly–Phe–Met
A

ENKEPHALINS

29
Q
  • binds
    receptors in the brain to reduce
    pain
A

Neurotransmitter

30
Q
  • Protects cellular
    contents from reactive oxygen
    species
A

Antioxidant

31
Q

protein –
only one peptide chain

A

Monomeric protein

32
Q

more than one peptide chain
(subunits)

A

Multimeric protein

33
Q

only AA
residues are present

A

Simple protein

34
Q

– one or
more peptide chains + one or
more

A

Conjugated protein

35
Q

2 fully extended protein chain segments in the same or different
molecules are held together by hydrogen bonds

A

BETA PLEATED SHEET

36
Q

– protein secondary structure that is neither an
⍺ helix nor a β pleated sheet

A

Unstructured segment

37
Q

Overall 3D shape of a protein due to the
interactions between amino acid
side chains (R groups)

A

Tertiary Structure

38
Q
  • Highest level of protein organization
  • Found only on multimeric proteins
A

Quaternary Structure

39
Q

Occurs when a protein or small peptide in a solution of strong acid or
base is heated

A

Hydrolysis

40
Q

– all peptide bonds are broken, freeing up all AAs

A

Complete hydrolysis

41
Q

– some, but not all peptide bonds are broken,
producing a mixture of free Aas and small peptides

A

Partial hydrolysis

42
Q

– enzyme-catalyzed hydrolysis of ingested proteins

A

Protein digestion

43
Q

Partial or complete disorganization of a protein’s characteristic 3D
shape due to disruption of its secondary, tertiary, or quaternary
structural interactions

A

Denaturation

44
Q
  • Protective coating for organism
  • Found in hair, fingernails,
    toenails, wool, feathers, claws
A

ALPHA KERATIN

45
Q
  • Most abundant protein
  • Found in skin, bones, tendons,
    ligaments, blood vessels
A

COLLAGEN

46
Q
  • Stores O2 in the muscles
  • Monomer that contains a
    heme group
A

MYOGLOBIN

47
Q
  • Transports O2 from the lungs to
    the tissue
  • Tetramer with each subunit
    containing a heme group
A

HEMOGLOBIN

48
Q

Conjugated protein produced by an
organism as a protective response to
specific foreign substances

A

Immunoglobulins

49
Q

Conjugated protein used to suspend lipids and
transport them through the bloodstream

A

Lipoproteins

50
Q
A

2ND YEAR MIDTERMS (6 decks)

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