PROTEINS Flashcards

1
Q

The word protein came from the Greek word _ which means first place. It is the most abundant organic molecule in the human body comprising more than 50% of the cell’s dry mass. It is composed of many amino acids bonded together via the peptide linkage thus providing a diverse range of functions

A

proteios

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2
Q

proteins that function for support, contraction, and movement

A

structural

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3
Q

proteins that bind and cary substances from one place to another

A

transport

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4
Q

proteins that enhance the rate of biochemical reaction

A

catalysis

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5
Q

proteins that desctroy invading pathogens and substances that can cause disease

A

defense

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6
Q

proteins that are released into the bloodstream and regulate the physiologic activities of their target cells

A

hormones

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7
Q

proteins that can be used in metabolic reactions that yield energy

A

energy source

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8
Q

The function of a protein is determined by its __.

A

structure

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9
Q

The overall three-dimensional shape of protein is known as its

A

native conformation

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10
Q

The structure of a protein has a maximum of four hierarchical levels

A

primary
secondary
tertiary
quaternary

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11
Q

hierarchy of protein structure
the amino acid sequence ofthe protein. this is the sole determinant of its overall shape (Anfinsen’s rule)

A

primary structure

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12
Q

hierarchy of protein structure
the local folding of protein segment into helical or sheet-like structure

A

secondary structure

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13
Q

hierarchy of protein structure
the compact three-dimensional structure or native conformaiton of proteins

A

tertiary structure

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14
Q

hierarchy of protein structure
involves the itneraction of the subunits of an oligomeric protein

A

quaternary

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15
Q

formed by the coiling of the polypeptide chain into a right-handed spiral

A

a-helix

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16
Q

formed when two adhacent chains of polypeptides forms H-bonds in an almost fully extended form thaat can be lkened to the pleats of an accordion

A

b-pleated sheet

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17
Q

the tertiary protein structure is stablized by (4)

A

H-bonds
salt bridges
hydrophobic interacitons
disulfide bridges

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18
Q

tertiary protein
are those that exist as fibers or sheets.
they are made up of one type of secondary structure and function for structural support
examples are collagen,mertain, and silk fibroin

A

fibrous protein

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19
Q

tertiary protein
are combinations of different secondary structures that are compactly folded into spherical shapes
examples are enzymes, myoglobin and hemoglobin

A

globular proteins

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20
Q

present into for oligomeric proteins like hemoglobin

A

quaternary

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21
Q

made up of more than 50 amino acids
100-10,000 amino acids linked together
polymers of amino acids

A

proteins

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22
Q

sources of protein (2)

A

complete proteins
incomplete proteins

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23
Q

sources of proteins
all essential amino acids present
beef, poultry, fish, eggs, soy

A

complete proteins

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24
Q

sources of proteins
nuts, seeds, beans

A

incomplete proteins

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25
Q

amino acid sequence of the protein

A

primary structure

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26
Q

secondary structure
coiling into right-handed spiral
10 turns 5.4 nanometers

A

a-helix

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27
Q

secondary structure
adjacent polypeptide chains form H bonds

A

B-pleted sheet

28
Q

secondary structure of proteins is stabilized by __

A

H-bonds

29
Q

protei nstructure
R groups of amino acids are involved

A

tertiary

30
Q

tertiary structure
slender
fibers or sheets
made up of type of secondary structure

A

fibrous

31
Q

tertiary strructure
spherical or compact
forms hydrophilic and hydrophobic regions
made up of different secondary structures

A

globular

32
Q

protein structure
found in multimeric/oligomeric proteins
composed of more than 1 subunit
itneraction of subunuts

A

quaternary

33
Q

1 amino acid in hemoglobin is wrong
Glutamic acid - Valine
change in structure = function

A

sickle cell disease

34
Q

normal protein
+
heat, acids, salts, and mechanical agitation

A

protein denaturation

35
Q

the quaternary structure is stabilized by

A

hydrophobic interactions

36
Q

the most abundant protein in the human body. It is the cementing component of various connective tissues like bones, tendons, ligaments, and skin.

A

collagen

37
Q

Collagen is a fibrous protein made up of __ that are twisted together to form a __. This structure can be likened to a rope made of three cords. Collagen is tough yet flexible.

A

three left-handed helices
right-handed super helix

38
Q

The primary structure of collagen is a repeating sequence of -__-__-__- where X is usually __ or sometimes lysine residue

A

–Gly-Pro-X-
4-hydroxyproline

39
Q

Severe deficiency in vitamin C leads to __ which is characterized by swelling & inflammation of the gums, impaired healing of wounds, loosening of the teeth, pain in joints, and progressive weakening of the body.

A

scurvy

40
Q

is the major fibrous protein in hair & nails, and a minor constituent of the skin. It is a component of the cells cytoskeleton that maintains their shape.

A

alpha keratin

41
Q

Alpha keratin is made up of __ that are twisted together to form a __.

A

two alpha-helices
left-handed super helix

42
Q

extensively stabilize the structure of keratin.

A

disulfide bridges

43
Q

are the carriers of oxygen in the muscles and the blood respectively.

A

myoglobin
hemoglobin

44
Q

Their basic composition is essentially the same, but myoglobin is made up of a __ while hemoglobin has four subunits. These subunits are designated as alpha1, alpha2, beta1, and beta2.

A

single unit

45
Q

Each subunit is made up of a nonprotein component or __

A

prosthetic group

46
Q

prosthetic group is the __ which consists of a tetrapyrole ring called __ with a coordinated Fe2+ atom.

A

heme group
porphyrin

47
Q

the protein component is called __ hence the term hemoglobin

A

globin

48
Q

is a peptide hormone that is produced by the beta cells of the pancreas (also known as islets of Langerhans) which stimulates the cells to uptake glucose from the blood, hence, lowering blood glucose level.

A

insulin

49
Q

insulin is a dimeric protein made up of __ and __ which contains __ and __ amino acid residues respectively, that are connected by __

A

A-chain
B-chain
21
30
two disulfide bonds

50
Q

insulin
The A-chain has two alpha helical regions at __ and __ which are antiparallel.

A

A1-A8
A12-A19

51
Q

insulin
B-chain has a __ structure from amino acid __ which are flanked by the disulfide bond on either sides and two beta sheets at amino acid B7-B10 and B20-B23

A

central alpha helical
B9-B19

52
Q

Deficiency in insulin production or resistance to insulin results to the __ which is a metabolic disorder that is characterized by hyperglycemia (high blood sugar) resulting to serious health complications like kidney failure, cardiovascular disease, stroke, nerve damage, and eye damage. Symptoms of diabetes mellitus includes frequent urination, increased thirst, impaired wound healing, and increased appetiteDeficiency in insulin production or resistance to insulin results to the diabetes mellitus which is a metabolic disorder that is characterized by _- (high blood sugar) resulting to serious health complications like kidney failure, cardiovascular disease, stroke, nerve damage, and eye damage. Symptoms includes frequent urination, increased thirst, impaired wound healing, and increased appetite

A

diabetes mellitus
hyperglycemia

53
Q

essential in hydroxylation
critical in maintaining structural integrity of collagen

A

vitamin c

54
Q

carrier of oxygen in th muscles
made up of a single unit

A

myoglobin

54
Q

it has a corkscrew shape that is dextral in nature
ten turns of the helix will cover a distance of 5.4 nanometers

A

alpha helix

55
Q

it results from decrease in insulin production by the pancreas or the cell’s insensitivity to insulin
it may manifest as polyphagia and polydipsia
it leads to fatal complications like chronic renal failure and cardiovascular diseases

A

diabetes mellitus

56
Q

it is the consequence of diet that is devoid of fruits and vegetables
it can be corrected by regular intake of ascorbic acid supplement

A

scurvy

57
Q

it is priimarily made up of achiral and cyclic amino acids
it is a dextral super helix hat is formed from three sinistral helices

A

collagen

58
Q

it a protein is predominantly made up of alipathic and aromatic amino acids, what can be true about it

A

it is most probably a structural protein
it is a protein that is hydrophobic in nature

59
Q

it hs 4 sub-units wit heach subunt binding an oxygen molecule in an increasing efficiency
it has ferrous cation that is coordinated by hte nucleophilic N atoms of the porphyrin ring

A

hemoglobin

60
Q

it is made up of 2 right-handed helices that are twisted together to form a sinistral usper helix

A

alpha keratin

61
Q

it is synthesized by the beta cells of the pancreas and released intothe bloodstream to stimulate assimilation by glucose by the cells
it is made u0p of 2 peptide chains with a total of 3 alpha helices, 3 beta sheeets, and 3 disulfide bridges

A

insulin

62
Q

reason why hydroxylation of proline residues is critical to the structural integrity of colllagen

A

the hydroxyl moities in Pro form H-bonds which stabilize collagen structure

63
Q

they are significantly hydrophilic in nature
they ae conflation of various types of local folding of polypeptide

A

globular proteins

64
Q

the sickle0shaped RBC’s are vaso-occluded in the capillaries resulting to damage in vairrous internal organs

A

sicke-cell anemia

65
Q

the stabilizing form or bond exhibited between Glu/Lys, and Phe/Val

A

ionic bond (salt bridge), and hydrophobic interactions