PROTEIN MAIN Flashcards

1
Q

an amino acid that contains one amino group and two carboxyl groups, the second carboxyl group being part of the side chain

A

Polar acidic

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2
Q

most abundant substances in nearly all cells

A

PROTEINS

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3
Q

what class of amino acids do these belong: D,E

A

Polar acidic

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4
Q

account for about __% of a cell’s overall mass and for almost half of a cell’s dry mass

A

15

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5
Q

a standard amino acid needed for protein synthesis that must be obtained from dietary sources because the human body cannot synthesize it in adequate amount

A

ESSENTIAL AA

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6
Q

average nitrogen content of proteins

A

15.4%

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7
Q

ESSENTIAL / NON:
R*,H,M,I,L,K,W,T,F,V

A

ESSENTIAL

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8
Q

typical human cell contains about how many different kinds of proteins

A

9 000

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9
Q

Synthesized by the body

A

NON-ESSENTIAL AMINO ACIDS

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10
Q

the human body contains about how many different proteins

A

100 000

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11
Q

ESSENTIAL / NON:
C,A,N,D,E,Y,S, Q,G,P

A

NON-ESSENTIAL

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12
Q

a naturally occurring, unbranched polymer in which the monomer units are amino acids

A

PROTEINS

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13
Q

a protein that contains all of the essential amino acids in the same relative amounts in which the body needs them

A

COMPLETE DIETARY PROTEIN

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14
Q

an amino acid in which the amino group, the carboxyl group and the hydrogen atom are attached to the a-carbon atom

A

a-amino acid

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15
Q

a protein that does not contain adequate amounts, relative to the body’s needs, of one or more of the essential amino acids

A

INCOMPLETE DIETARY PROTEIN

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16
Q

TRUE / FALSE:
All amino acids are alpha-amino acids except Valine (an imino acid) since the side chain is not free but attached to the amino group

A

FALSE, PROLINE

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17
Q

an 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

CLASSIFICATION OF AMINO ACIDS

A

1) Nonpolar amino acid
2) Polar neutral
3) Polar basic
4) Polar acidic

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19
Q

two or more incomplete dietary proteins that, when combined, provide an adequate amount of all essential amino acids relative to the body’s needs

A

COMPLEMENTARY DIETARY PROTEINS

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20
Q

an amino acid that contains one amino group, one carboxyl group, and a nonpolar side chain

A

Nonpolar amino acid

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21
Q

pure form of amino acids

A

white crystalline solids with relatively high decomposition points

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22
Q

what class of amino acids do these belong: G,A,V,L,I,P,F,M,W

A

Nonpolar amino acid

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23
Q

TRUE / FALSE:
most amino acids are not very soluble in water because of strong intermolecular forces within their crystal structures

A

TRUE

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24
Q

an amino acid that contains one amino group, one carboxyl group, and a side chain that is polar but neutral

A

Polar neutral

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25
Q

a molecule that has a positive charge on one atom and a negative charge on another atom, but which has no net charge

A

Zwitterion

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26
Q

what class of amino acids do these belong: S,C,N,T,Q,Y

A

Polar neutral

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27
Q

net charge on a zwitterion is?

A

ZERO

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28
Q

an amino acid that contains two amino groups and one carboxyl group, the second amino group being part of the side chain

A

Polar basic

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29
Q

in a sol’n three diff aa forms can exist namely?

A
  • zwitterion
  • nega ion
  • posi ion
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30
Q

what class of amino acids do these belong: H,K,R

A

POLAR BASIC

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31
Q

an example of this protein is insulin

A

MULTIMERIC PROTEIN

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32
Q

important pH value, relative to the various forms an amino acid can have in a solution

A

ISOELECTRIC POINT

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33
Q

a protein in which only amino acid residues are present

A

SIMPLE PROTEIN

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34
Q

pH at which an aa exist primarily in its zwitterion form

A

ISOELECTRIC POINT

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35
Q

a protein that has one or more non-amino acid entities present in its structure in addition to one or more peptide chains

A

CONJUGATED PROTEIN

36
Q

formed by a biochemical reaction that extracts a water (H2O) molecule as it joins the amino group of one amino acid to the carboxyl group of a neighboring amino acid

A

Peptide bonds

37
Q

include substances formed from simple conjugated proteins

A

DERIVED PROTEIN

38
Q

another term for Peptide bond

A

AMIDE BOND

39
Q

Protein whose molecules have an elongated shape with one dimension much longer than the others

A

FIBROUS

40
Q

a covalent bond between the carboxyl group of one amino acid and the amino group of another amino acid

A

PEPTIDE BOND

41
Q

Tend to have simple, regular and linear structures

A

FIBROUS

42
Q

TRUE / FALSE:
The smallest group of amino acids have nonpolar side chains

A

FALSE, LARGEST

43
Q

Molecular weights are high and its function is for structural and support (class of proteins based on shape)

A

FIBROUS

44
Q

TRUE / FALSE:
cysteines are the only amino acids capable of forming covalent bonds

A

TRUE

45
Q

molecules have peptide chains that are folded into spherical or globular shapes

A

GLOBULAR

46
Q

TYPES OF PEPTIDE BOND

A

1) Dipeptide
2) Tripeptide
3) oligopeptide
4) Polypeptide

47
Q

most of amino acids with hydrophobic side chains (nonpolar R groups) are in the interior of the molecules and most of the hydrophilic side chains (polar) are on the outside of the molecule

A

GLOBULAR

48
Q

type of peptide w/ 2 or more amino acids

A

Dipeptide

49
Q

Soluble in aqeous media, Have been crystallized and have definite molecular weights and can be denatured

A

GLOBULAR

50
Q

type of peptide w/ 3 or more amino acids joined together in a chain

A

Tripeptide

51
Q

occurs when protein deprivation is relatively greater than the reduction in total calories

A

Kwashiorkor

52
Q

type of peptide w/ 10 or 20 amino acid residues are present in a chain

A

oligopeptide

53
Q

frequently seen in children after weaning at about one year of age, when their diet consists predominantly of carbohydrates

A

Kwashiorkor

54
Q

type of peptide w/ longer unbranched chain of amino acids

A

Polypeptide

55
Q

Typical symptoms include stunted growth, edema, skin lesions, depigmented hair, anorexia, enlarged fatty liver, and decreased plasma albumin concentration

A

Kwashiorkor

56
Q

TSH meaning

A

THYROID STIMULATING HORMONE

57
Q

state some typical symtpoms of Kwashiorkor

A

stunted growth
edema
skin lesions
depigmented hair
anorexia
enlarged fatty liver
decreased plasma albumin concentration

58
Q

primary structure of a protein

A

amino acid sequence

58
Q

CLASSIFICATION OF PROTEINS

A

1) NUMBER OF PEPTIDE CHAIN
2) CHEMICAL COMPOSITION
3) BASED ON SHAPE

58
Q

occurs when calorie deprivation is relatively greater than the
reduction in protein

A

Marasmus

59
Q

usually occurs in children younger than 1 year of age when breast milk is supplemented with watery gruels of native cereals that are usually deficient in protein and calories

A

Marasmus

59
Q

sub class of NUMBER OF PEPTIDE CHAIN

A

MONOMERIC PROTEIN
MULTIMERIC PROTEIN

59
Q

a protein in which only one peptide chain is present

A

MONOMERIC PROTEIN

60
Q

Typical symptoms include arrested growth, extreme muscle wasting (emaciation), weakness, and anemia

A

Marasmus

61
Q

an example of this protein is myoglobin

A

MONOMERIC PROTEIN

61
Q

amyloid plaque caused by accumulation of amyloid β (Aβ)

A

Alzheimer disease

62
Q

state some typical symtpoms of Marasmus

A

arrested growth
extreme muscle wasting (emaciation)
weakness
anemia

62
Q

a protein in which more than one peptide chain is present

A

MULTIMERIC PROTEIN

63
Q

The peptide chains present are called protein subunits

A

MULTIMERIC PROTEIN

63
Q

when patient digests too much cyanide and may cause the blood to turn into a chocolate-like colored substance

A

methemoglobinemia / chocolate cyanosis

63
Q

a peptide containing 40–42 amino acid residues, which are nonbranching fibrils of Beta pleated sheet

A

amyloid β (Aβ)

64
Q

Alzheimer disease is when there is an amyloid plaque caused by accumulation of?

A

amyloid β (Aβ)

65
Q

accumulation of neurofibrillary tangles inside neurons

A

Alzheimer disease

65
Q

accumulation of insoluble, long, fibrillar protein assemblies consisting of β-pleated sheets caused by abnormal proteolytic cleavage

A

Amyloidosis

65
Q

prion protein (PrP or PRNP) has been strongly implicated as the causative agent of transmissible spongiform encephalopathies

A

Prion disease

65
Q

Prion disease in humans

A

Creutzfeldt-Jakob disease

65
Q

Prion disease in sheep

A

scrapie

65
Q

Prion disease in cattle

A

bovine spongiform encephalopathy / mad cow disease

65
Q

type of CJD where there is a mutation in PRNP gene at the 200th codon, causing conversion of glutamic acid to lysine

A

Familia CJD

66
Q

Types of CJD

A

1) Familia CJD
2) Variant CJD
3) Iatrogenic CJD
4) Sporadic CJD

66
Q

increased concentration of 14-3-3 protein in cerebrospinal fluid

A

Creutzfeldt-Jakob disease

66
Q

type of CJD where eating cow’s meat with prion protein

A

Variant CJD

67
Q

type of CJD where it is caused by medical procedure (exx. Corneal transplant)

A

Iatrogenic CJD

67
Q

type of CJD w/ no clear cause but spontaneous mutation in the 129th codon of the PRNP gene causing replacement of valine to methionine

A

Sporadic CJD

68
Q

TSE meaning

A

transmissible spongiform encephalopathies

69
Q

cannibalism of infected flesh (like fatal familial insomnia caused by mutation of PRNP gene at the 178th codon replacing aspartic acid with asparagine)

A

kuru disease