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
amino acid sequence of the protein
primary structure
26
secondary structure coiling into right-handed spiral 10 turns 5.4 nanometers
a-helix
27
secondary structure adjacent polypeptide chains form H bonds
B-pleted sheet
28
secondary structure of proteins is stabilized by __
H-bonds
29
protei nstructure R groups of amino acids are involved
tertiary
30
tertiary structure slender fibers or sheets made up of type of secondary structure
fibrous
31
tertiary strructure spherical or compact forms hydrophilic and hydrophobic regions made up of different secondary structures
globular
32
protein structure found in multimeric/oligomeric proteins composed of more than 1 subunit itneraction of subunuts
quaternary
33
1 amino acid in hemoglobin is wrong Glutamic acid - Valine change in structure = function
sickle cell disease
34
normal protein + heat, acids, salts, and mechanical agitation
protein denaturation
35
the quaternary structure is stabilized by
hydrophobic interactions
36
the most abundant protein in the human body. It is the cementing component of various connective tissues like bones, tendons, ligaments, and skin.
collagen
37
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.
three left-handed helices right-handed super helix
38
The primary structure of collagen is a repeating sequence of -__-__-__- where X is usually __ or sometimes lysine residue
–Gly-Pro-X- 4-hydroxyproline
39
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.
scurvy
40
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.
alpha keratin
41
Alpha keratin is made up of __ that are twisted together to form a __.
two alpha-helices left-handed super helix
42
extensively stabilize the structure of keratin.
disulfide bridges
43
are the carriers of oxygen in the muscles and the blood respectively.
myoglobin hemoglobin
44
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.
single unit
45
Each subunit is made up of a nonprotein component or __
prosthetic group
46
prosthetic group is the __ which consists of a tetrapyrole ring called __ with a coordinated Fe2+ atom.
heme group porphyrin
47
the protein component is called __ hence the term hemoglobin
globin
48
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.
insulin
49
insulin is a dimeric protein made up of __ and __ which contains __ and __ amino acid residues respectively, that are connected by __
A-chain B-chain 21 30 two disulfide bonds
50
insulin The A-chain has two alpha helical regions at __ and __ which are antiparallel.
A1-A8 A12-A19
51
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
central alpha helical B9-B19
52
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
diabetes mellitus hyperglycemia
53
essential in hydroxylation critical in maintaining structural integrity of collagen
vitamin c
54
carrier of oxygen in th muscles made up of a single unit
myoglobin
54
it has a corkscrew shape that is dextral in nature ten turns of the helix will cover a distance of 5.4 nanometers
alpha helix
55
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
diabetes mellitus
56
it is the consequence of diet that is devoid of fruits and vegetables it can be corrected by regular intake of ascorbic acid supplement
scurvy
57
it is priimarily made up of achiral and cyclic amino acids it is a dextral super helix hat is formed from three sinistral helices
collagen
58
it a protein is predominantly made up of alipathic and aromatic amino acids, what can be true about it
it is most probably a structural protein it is a protein that is hydrophobic in nature
59
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
hemoglobin
60
it is made up of 2 right-handed helices that are twisted together to form a sinistral usper helix
alpha keratin
61
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
insulin
62
reason why hydroxylation of proline residues is critical to the structural integrity of colllagen
the hydroxyl moities in Pro form H-bonds which stabilize collagen structure
63
they are significantly hydrophilic in nature they ae conflation of various types of local folding of polypeptide
globular proteins
64
the sickle0shaped RBC's are vaso-occluded in the capillaries resulting to damage in vairrous internal organs
sicke-cell anemia
65
the stabilizing form or bond exhibited between Glu/Lys, and Phe/Val
ionic bond (salt bridge), and hydrophobic interactions