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BioChem for MedTech > Proteins > Flashcards

Proteins Flashcards

1
Q

Is an unbranched chain of amino acids, each joined to the next by a peptide bond

A

Peptide

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2
Q

True or False.

Inorganic proteins consists of Phosphoproteins, Metalloproteins, and Hemoproteins

A

False, Hemoproteins is included in Organic

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3
Q

Consists all the essential amino acids in approximately the same relative amounts in which the human body needs them

A

Complete dietary protein

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4
Q

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

A

Zwitterion

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5
Q

True or False.
Zwitterion proteins does not change its own pH but rather changes the charges of ions between an amino group and carboxyl group

A

False, they change in pH but does not change in charge

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6
Q

It is an amino acid in which the amino group and the carboxyl group are attached to the alpha-carbon atom

A

Alpha-amino acid

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7
Q

It is an organic compound that contains both an amino group and carboxyl group

A

Amino Acid

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8
Q

True or False.

The side chain (R group) distinguishes alpha-amino acids from each other by chemical means only

A

False, both physically and chemically

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9
Q

True or False.

According to the rule for drawing the Fischer projection of amino acids, the carboxyl group as in a horizontal position

A

False, is at the top of the projection

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10
Q

True or False.
According to the rule of drawing for Fischer Projection, the amino group is the only one who can denote whether an amino acid is levorotatory or dextrorotatory

A

True

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11
Q

It is the only standard amino acid that has a side chain that contains a thiol (-SH) group

A

Cysteine

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12
Q

If a cysteine is oxidized, it dimerizes to another cysteine to form what?

A

Cystine molecule

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13
Q

It is necessary in most metabolic processes of the human body that the body itself cannot synthesize

A

Essential amino acid

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14
Q

The strongest of the tertiary-structure interactions A result from the thiol groups of two cysteine residues reacting with each other.

A

Disulfide Bond

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15
Q

True or False

Disulfide Bond is an Ionic Bond

A

False, Covalent Bond

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16
Q

It occurs between amino acids with polar R groups

A

Hydrogen Bond

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17
Q

It results when two nonpolar side chains are close to each other

A

Hydrophobic interactions

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18
Q

It always involve the interaction between an acidic side chain and a basic side chain

A

Electrostatic Interactions (salt bridges)

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19
Q

It is the organization among the the various peptide chains in a multimeric protein.

A

Quaternary protein structure

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20
Q 
Morse Type
A quaternary protein structure consists of:
I. Electrostatic Attractions
II. Hydrogen Bonds
III. Disulfide Bond
IV. Hydrophobic Bond

A. II, III, IV
B. I, II, III, IV
C. I, II, IV
D. I, II, III

A

C. I, II, IV

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21
Q

It is a single protein chain that adopts a shape which resembles a coiled spring (helix), with the coil configuration maintained by hydrogen bonds

A

Alpha helix structure

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22
Q 
Morse Type
A secondary protein has two types depending on the on the manner of hydrogen bonding:
I. Gamma Pleated Helix
II. Omega Coiled Spring
III. Alpha Helix
IV.  Beta Pleated Sheet

A. I, II, IV
B. II, III
C. I, II, III
D. III, IV

A

D. III, IV

23
Q

True or False.

The amino acid sequence of myoglobin is identical to all the myoglobin of the body

24
Q

True or False.

Pigs, Cows, Horses, and Human have similarities in the sequence of insulin amino acid

25
Q

Are molecules that have an elongated shape with one dimension much longer than the others

A

Fibrous protein

26
Q

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

A

Globular protein

27
Q

A kind of protein based on shape which is associated with a membrane system of a cell

A

Membrane Protein

28
Q

True or False.

The sequence of amino acids present in a protein’s peptide chain or chains is a secondary structure

A

False, Primary Structure

29
Q

The overall three-dimensional shape that results form the attractive forces between amino acid side chains (R groups) that are not near each other in the protein chain

A

Tertiary Structure

30
Q

True or False.

A protein with only the amino acid residues are present is called Complex (conjugated) protein

A

False, Simple Protein

31
Q

True or False.

A protein is made up of at least 35 alpha-amino acid residues

A

False, 40 alpha-amino acid residues

32
Q

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

33
Q

True or False.
Difference in molecules contain the same amino acids but in different order are called Enantiomeric Peptides.

Ex. Ala-Gly and Gly-Ala

A

False, Isomeric Peptides

34
Q

It is an amide bond between amino acids. It is also a covalent bond between the carboxyl group of one amino acids and the amino group of another amino acid

A

Peptide Bond

35
Q

It is a portion of an amino acid structure that remains, after the release of H20, when an amino acid participates in peptide bond formation as it becomes part of a peptide chain

A

Amino acid residue

36
Q

A peptide with 3 amino acid chains

A

Tripeptide

37
Q

A peptide with 2 amino acid chains

38
Q

A peptide with 10 to 20 amino acid chains

A

Oligopeptide

39
Q

A peptide with more than 20 amino acid chains

A

Polypeptide

40
Q

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

A

Polar Basic Amino Acid

41
Q

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

A

Polar Acidic Amino Acid

42
Q

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

A

Polar Neutral Amino Acid

43
Q

It contains one amino group, one carboxyl group, and a nonpolar side chain.

A

Nonpolar amino acid

44
Q

True or False.
A tertiary consists of four (4) types of peptide unit interactions namely covalent disulfide bonds, hydrogen bonds, hydrophobic attractions, and electrostatic attractions (salt bridges)

45
Q

It is a two fully extended protein chain segments in the same or different molecules that are held together by hydrogen bonds

A

Beta pleated sheet structure

46
Q

A protein with only amino acid residues are present

A

Simple protein

47
Q

A protein that has non-amino acid entity (prosthetic group) present in its structure

A

Complex (conjugated) protein

48
Q

Lipoproteins, Glycoproteins, Hemoproteins, and Nucleoproteins are?

49
Q

Metalloproteins and Phosphoproteins are?

50
Q

A protein that has more than one peptide chain

A

Multimeric protein

51
Q

A protein that has only one peptide chain

A

Monomeric protein

52
Q

True or False.

In primary protein structure, the order of attachment of amino acids are linked together in protein

53
Q

The overall three-dimensional shape of a protein that results from the interactions between amino acid side chains that are widely separated from each other within a peptide chain

A

Tertiary protein structure

BioChem for MedTech (3 decks)

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