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BIOCHEMISTRY > PROTEINS > Flashcards

PROTEINS Flashcards

1
Q

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

A

Protein

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2
Q

is an amino acid in which the amino group and the carboxyl group are
attached to the a-carbon atom. The general structural formula for a amino acid is

A

a Amino acid

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3
Q

is one of the 20 a-amino acids normally found in proteins

A

standard amino acid

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4
Q

is an amino acid that contains one amino group, one
carboxyl group, and a nonpolar side chain. When incorporated into a protein, such amino
acids are hydrophobic (“water-fearing”)

A

Nonpolar amino acids

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5
Q

is an amino acid that contains one amino group, one
carboxyl group, and a side chain that is polar but neutral. polar neutral amino acid is neither acidic nor basic

A

polar neutral amino acid

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6
Q

is an amino acid that contains one amino group and
two carboxyl groups, the second being part of the side chain. side chain of a polar acidic amino acid bears a negative charge

A

Polar Acidic amino acids

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7
Q

is an amino acid that contains two amino groups and
one carboxyl group, the second amino group being part of the side chain. , the side chain of a polar basic amino acid bears a positive charge.

A

Polar basic amino acid.

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8
Q

List all the amino acids of Nonpolar

A

Glycine, alanine, valine, leucine, Isoleucine, proline, Phenylalanine, methionine, tryptophan.

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9
Q

lists all the amino acids of the polar acidic amino acid

A

Aspartic acid and Glutamic Acid

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9
Q

list all the amino acids in polar neutral amino acids

A

threonine, tyrosine, cysteine, asparagine, glutamine.

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10
Q

List all the amino acids of the polar basic amino acids

A

Histidine, lysine, Arginine.

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11
Q

List all down the 11 essential amino acid

A

Arginine, histidine, isoleucine, leucine, lysine, methionine, phenylalanine, valine, threonine, tryptophan, valine.

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12
Q

is a protein that contains 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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13
Q

is an amino acid needed in the human
body that must be obtained from dietary sources because it cannot
be synthesized within the body from other substances in adequate
amounts

A

essential amino acid

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14
Q

the simplest of the standard
amino acids, is achiral. All of the
other standard amino acids are chiral.

A

Glycine

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14
Q

carboxyl groups tend to lose
protons (H+) they will have?

A

producing a negatively charged species

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15
Q

, amino groups have a tendency to accept protons (H+) they will have

A

producing a positively charged species

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16
Q

is 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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17
Q

Strong intermolecular forces between
the positive and negative centers of
zwitterions are the cause of the high?

A

Melting points of amino acids

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18
Q

is the pH at which an amino acid solution has no net charge because an
equal number of positive and negative charges are present

A

Isoelectric Point

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19
Q

Isoelectric point from what range?

A

4.8 to 6.3

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20
Q

is the process of separating charged molecules on the basis of their migration toward charged electrodes associated with an electric field.

A

Electrophoresis

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21
Q

that has a side chain that contains a sulfhydryl group

A

Cysteine.

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22
Q

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

A

peptide

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23
Q

is a long unbranched chain of amino acids, each joined to the next by a peptide bond

A

polypeptide

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24
Q

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

A

Peptide bond

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25
Q

is the portion of an amino acid structure that remains, after the release of H2O, when an amino acid participates in peptide bond formation as it becomes part of a peptide chain.

A

Amino acid residues.

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26
Q

the same amino acids but in different order are different molecules
(constitutional isomers) with different properties

A

Isomeric Peptides

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27
Q

The two best-known peptide hormones, both produced by the pituitary gland.

A

oxytocin and vasopressin

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28
Q

plays a role in stimulating
the flow of milk in a nursing mother

A

Oxytocin

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29
Q

are pentapeptide neurotransmitters produced by the brain itself that bind at
receptor sites in the brain to reduce pain

A

Enkephalins

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30
Q

is a protein in which
only one peptide chain is present

A

monomeric protein

31
Q

is a protein in which more than one
peptide chain is present

A

multimeric protein

32
Q

The peptide chains present in multimeric proteins are called

A

Protein subunits

33
Q

is a protein in which only amino acid residues are present

A

simple protein

34
Q

is a protein that has one or more nonomino acid entities present in its structure in addition to one or more peptide chains

A

conjugated protein

35
Q

non-amino acid group present in a conjugated protein.

A

prosthetic group

36
Q

is the order in which amino acids are linked together in a protein

A

Primary protein structure

37
Q

is the arrangement in space adopted by the backbone portion of a protein

A

Secondary protein structure

38
Q

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

A

alpha helix structure

39
Q

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

A

beta-pleated sheet structure

40
Q

used in describing portions of a protein structure is somewhat of a misnomer because all molecules of a given protein exhibit identical unstructured segment

A

Unstructured

41
Q

is the overall three-dimensional shape of a protein that results from the interactions between amino acid side chains

A

Tertiary protein structure

42
Q

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

A

Quaternary protein structure

43
Q

The regularly repeating ordered
spatial arrangements of amino
acids near each other in the
protein chain, which result from
hydrogen bonds between
carbonyl oxygen atoms and
amino hydrogen atoms

A

SECONDARY
STRUCTURE

44
Q

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

A

PRIMARY
STRUCTURE

45
Q

Hydrogen bonds between two
side-by-side chains, or a single
chain that is folded back on
itself

A

Beta Pleated Sheet

46
Q

Hydrogen bonds between
every fourth amino acid

A

ALPHA HELIX

47
Q

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

A

TERTIARY
STRUCTURE

48
Q

The three-dimensional shape of a
protein consisting of two or more
independent peptide chains,
which results from noncovalent
interactions between R group

A

QUATERNARY
STRUCTURE

48
Q

is a protein whose molecules have an elongated shape with one dimension much longer than the others

A

fibrous protein

49
Q

is a protein whose molecules have peptide chains that are folded into spherical or globular shapes

A

globular protein

50
Q

is a protein that is found associated with a membrane system of a cell

A

Membrane Protein

51
Q

is particularly abundant in nature, where it is found in protective
coatings for organisms

A

Keratin

52
Q

the most abundant of all proteins in humans (30% of total body protein), is a
major structural material in tendons, ligaments, blood vessels, and skin

A

Collagen

53
Q

transports oxygen from the lungs to tissue

A

Hemoglobin

53
Q

Proteins are probably best known for their role as catalysts

A

Catalytic proteins

54
Q

functions as an oxygen storage molecule in muscles

A

Myoglobin

55
Q

These proteins, also called immunoglobulins or antibodies are central to the functioning of the body’s immune system. They bind to foreign substances, such as bacteria and viruses, to help combat invasion of the body by foreign particles.

A

Defense Proteins

56
Q

These proteins bind to particular small biomolecules and transport them to other locations in the body and then release the small molecules as needed at the destination location

A

Transport proteins

56
Q

These proteins transmit signals to coordinate biochemical processes between different cells, tissues, and organs that regulate body processes are messenger proteins, including
insulin and glucagon

A

Messenger proteins.

56
Q

These proteins confer stiffness and rigidity to otherwise fluidlike biochemical systems. Collagen is a component of cartilage, and a keratin gives mechanical strength as well as a protective covering
to hair, fingernails, feathers, hooves, and some animal shells.

A

Structural proteins

57
Q

These proteins are necessary for all forms of movement. Muscles are composed of filament-like contractile proteins that, in response to
nerve stimuli, undergo conformation changes that involve contraction and extension. Sperm can “swim” because of long flagella made up of contractile proteins.

A

Contractile proteins.

58
Q

help control the movement of small molecules and ions through the cell
membrane

A

Transmembrane proteins

59
Q

These proteins are often found “embedded” in the exterior surface of cell membranes. They act as sites at which messenger molecules, including messenger proteins such as insulin, can bind and thereby initiate the effect that the messenger “carries.”

A

Regulatory proteins.

59
Q

These proteins bind (and store) small molecules for future use. During the degradation of hemoglobin, the iron atoms present are released and become part of ferritin, an iron-storage protein, which saves the iron for
use in the biosynthesis of new hemoglobin molecules.

A

Storage proteins

60
Q

These proteins are particularly important in the early stages of
life, from embryo to infant. Casein, found in milk, and ovalbumin, found in egg white, are two examples of such proteins

A

Nutrient proteins.

61
Q

is the partial or complete disorganization of a protein’s characteristic three-dimensional shape as a result of disruption of its secondary, tertiary, and quaternary structural interactions

A

Protein denaturation

62
Q

is a protein that contains carbohydrates or carbohydrate derivatives in
addition to amino acids

A

Glycoproteins

63
Q

is a glycoprotein produced by an organism as a protective response to the invasion of microorganisms or foreign molecules

A

Immunoglobulins

64
Q

is a foreign substance, such as a bacterium or virus, that invades the human body

A

Antigens

65
Q

is a conjugated protein that contains lipids in addition to amino acids

A

lipoprotein

66
Q

is a biochemical molecule that counteracts a specific antigen.

A

Antibody

67
Q

is a lipoprotein that is involved in the transport system for
lipids in the bloodstream.

A

plasma lipoprotein

68
Q

Their function is to transport dietary triacylglycerols from the
intestine to the liver and to adipose tissue

A

Chylomicrons.

69
Q

Their function is to transport cholesterol synthesized in the liver to cells throughout the body.

A

Low-density lipoproteins (LDL)

69
Q

Their function is to transport triacylglycerols synthesized in the liver to adipose tissue.

A

Very-low-density lipoproteins (VLDL)

70
Q

Their function is to collect excess cholesterol from body tissues and transport it back to the liver for degradation to bile
acids

A

High-density lipoproteins (HDL)

BIOCHEMISTRY (8 decks)

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