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Proteins > Protein > Flashcards

Protein Flashcards

1
Q

are macromolecules made of amino acids, with each amino acid being linked to another via a peptide bond.

A

Proteins

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2
Q

proteins can bear positive & negative charges

A

amphoteric

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3
Q

synthesized in the liver & secreted by the hepatocyte
into the circulation EXCEPT immunoglobulins

A

plasma cells

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4
Q

provide ________ of the total daily body energy
requirement

A

12 – 20%

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5
Q

composes __________ of the cell’s dry weight

A

50 – 70%

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6
Q

is formed when the carboxyl (-COOH) group of one amino acid links to the amino (-NH2) group of another amino acid with the loss of a water molecule.

A

Peptide bond

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7
Q

End of protein structure with a free amino group

A

N-terminal

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8
Q

End of protein structure with a free carboxyl group

A

C-terminal

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9
Q

Proteins consist of 16% nitrogen, which differentiates proteins from carbohydrates and lipids.

A

Nitrogen content

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10
Q

Structure of an Amino Acid

A

Peptide bond
N-terminal
C-terminal
Nitrogen content

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11
Q

maintenance of water distribution between cells and tissue, interstitial compartments, and the vascular system of the body(________)

A

Osmotic force
Albumin

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12
Q

participation as buffers to maintain pH

A

Acid-base balance

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13
Q

metabolic substances (Albumin, Haptoglobin, Transferrin)

A

Transport
(Albumin, Haptoglobin, Transferrin)

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14
Q

part of immune defense system (________________/ _________________)

A

Antibodies
(Gammaglobulins/ Immunoglobulins)

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15
Q

Five major classes of antibodies

A

IgA, IgD, IgE, IgG, and IgM

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16
Q

Synthesized in plasma cells as an immune response

A

Antibodies

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17
Q

______________ and receptors (Peptide hormones: Insulin, glucagon, thyrocalcitonin, pituitary hormones (GH, PTH, PRL), and hypothalamic (ADH, oxytocin, thyrotropin releasing
hormones)

A

Hormones

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18
Q

Peptide hormones

A

Insulin, glucagon, thyrocalcitonin, pituitary hormones, hypothalamic

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19
Q

3 pituitary hormones

A

Growth Hormone (GH), Pituitary Hormone (PTH), Prolactin (PRL)

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20
Q

3 hypothalamic

A

ADH, oxytocin, thyrotropin releasing hormones

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21
Q

connective tissue (___________, _______, ____________)

A

Structure
(collagen, keratin, elastic fibers)

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22
Q

catalysts (_______________, _________, _______________)

A

Enzymes
(Dehydrogenases, kinase, phosphatase)

23
Q

participation in coagulation of blood (____________)

A

Hemostasis
(Fibrinogen)

24
Q

Proteins can be broken down into amino acids that can be used in the citric acid cycle to produce energy.

A

Energy

25
Q
  • linear sequence of the AA
    − basis for differentiation
    − analytical processes : ______________, _______________, _____________and ____________________
A

Primary Structure
(chromatography, electrophoresis, dye binding and light absorbance depend on this sequence)

26
Q

refers to the specific regular recurring arrangement in space of the
primary structure extending along one dimension

A

Secondary structure

27
Q

three structures : (dependent on numerous hydrogen bonds and occasional disulfide covalent bonds)

A

alpha-helix, beta-pleated sheets, random coils

28
Q

chain forms a regular helix ; coil resembling a spring

A

alpha-helix

29
Q

in fully extended structures; flat, corrugated structure

A

beta-pleated sheets

30
Q

no apparent pattern

A

random coils

31
Q

actual 3-dimensional structure or folding pattern of the protein, uniquely determined by its AA sequence leading to a specific shape

A

Tertiary structure

32
Q

Tertiary structure is maintained by ______________________, ______________, _________________ (_______________) and _____________________

A

electrovalent linkages, hydrogen bonds, disulfide bridges (covalent disulfide) and hydrophobic interactions

33
Q

combination of subunits

A

Quaternary structure

34
Q
  • association of several polypeptide chains into larger “oligomeric” aggregate unit
  • stable complexes : ______, _______, _________
A

Quaternary structure
(dimers, trimers, tetramers)

35
Q

chemically react as either acid or base

A

Amphoteric

36
Q

readily modified in solution when subjected to alterations in pH, UVR, heat and organic
solvents

A

Labile

37
Q

_______________ & _______________ due to the presence of side chains & active NH2 groups

A

Very reactive & highly specific

38
Q

3 Solubility

A

neutral salt, pH, organic solvents

39
Q

low salt concentration increases solubility of CHONs

A

Salting in

40
Q

high salt level concentration decreases solubility of CHONs

A

Salting out

41
Q

In metallic poisoning, __________ and ____ will precipitate the
metals

A

egg white and milk

42
Q

solubility is minimum at isoelectric point (when molecule has the no net charge) and solubility rises with increasing acidity or alkalinity

A

pH

43
Q

decreases solubility

A

Organic solvents

44
Q

Selective separation of the constituent proteins of a mixture can be achieved by proper adjustment of __, _______________, __________________________, _________________ and __________________
kept at low level.

A

Fractionation
(pH, temperature, alcohol concentration, protein concentration and salt concentration)

45
Q

2 Action of heat

A

Denaturation, Coagulation

46
Q

proteins undergo slight intramolecular rearrangements when they are heated between _________ (_____________)

A

Denaturation
40 – 50° (reversible)

47
Q

linkage of adjacent protein molecules by means of Hydrogen bonds (further heating will cause _______________ damage)

A

Coagulation
(irreversible)

48
Q

3 Precipitation

A

By acids, By salts of heavy metals, By alcohol

49
Q

negative charged acids neutralizes the positively charge proteins formation of insoluble salts

A

By acids

50
Q

formation of insoluble salts

A

By salts of heavy metals

51
Q

Example salts of heavy metals

A

(alkali metals; Hg, Ag and Pb)

52
Q

precipitation occurs as isoelectric point

A

By alcohol (dehydration)

53
Q

Alcohol precipitates bacteria (antiseptic property) at ___

A

70%

Proteins (2 decks)

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