Protein Flashcards

1
Q

It is a large biological molecule
made of many amino acids linked together
through amide (peptide) bonds.

A

Proteins

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2
Q

the second most abundant substances in nearly all cells (15% of cell’s overall mass)

A

Proteins

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3
Q

4 elements in protein

A

element of carbon, hydrogen, oxygen, and
nitrogen

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4
Q

how many amino acid residue are at least present in a protein

A

40 amino acids

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5
Q

how many amino acid residues are common in protein

A

400-500

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6
Q

how many small proteins contains?

A

40-100 amino acid residue

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7
Q

a protein in which only one
peptide chain is present

A

monomeric protein

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8
Q

a protein in which more than
one peptide chain is present
(insulin)

A

multimeric protein

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9
Q

protein subunits are ___

A

peptide chains present in
multimeric proteins

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10
Q

two types of protein chem comopistion

A

simple and conjugated protein

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11
Q

it is a protein that has one or
more non-amino-acid entities
present

A

conjugated protein

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12
Q

is a protein in which only
amino acid residues are
present

A

simple protein

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13
Q

a non-amino-acid group present in a
conjugated protein is called

A

prosthetic group

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14
Q

the sequence in which its amino
acids are lined up and connected by peptide bonds

A

Primary Protein Structure

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15
Q

(also called N-terminal amino acid, the one with the free -NH3+) on the LEFT

A

amino-terminal amino acid

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16
Q

(also called the C-terminal amino acid, the
one with the free -COO-) on the RIGHT

A

carboxyl-terminal amino acid group

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17
Q

true or false

So crucial is primary structure to function—no matter how big the
protein—that the change of only one amino acid can sometimes drastically alter a protein’s biological properties.

A

true

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18
Q

a hereditary disease caused by a genetic
difference that replaces one amino acid
(glutamate, Glu) with another (valine, Val) in
each of two polypeptide chains of the hemoglobin
molecule

A

Sickled-cell Anemia

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19
Q

Regular and repeating structural
patterns of alpha helix or beta sheet
created by hydrogen bonding between
backbone atoms in neighboring
segments of protein chains.

A

Secondary Protein Structure

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20
Q

a protein chain forms a
right-handed coil stabilized by
hydrogen bonds between peptide
groups along its backbone.

A

alpha-helix (α-helix)

21
Q

Secondary protein structure in which
adjacent protein chains either in the
same molecule or in different
molecules are held together by
hydrogen bonds along the
backbones, forming a flat sheet-like
structure.

A

beta-sheet (β-sheet)

22
Q

Secondary protein structure in which
adjacent protein chains either in the
same molecule or in different
molecules are held together by
hydrogen bonds along the
backbones, forming a flat sheet-like
structure.

A

beta-sheet (β-sheet)

23
Q

what is unstructured segments?

A

portions of a protein that have neither
alpha helix nor beta pleated sheet
structure

24
Q

The way in which an entire
protein chain is coiled and
folded into its specific three-
dimensional shape.

A

Tertiary protein structure

25
4 Interactions Responsible for Tertiary Structure
1. covalent disulfide bonds, 2. electrostatic attractions (salt bridges), 3. hydrogen bonds, and 4. hydrophobic attractions
26
involves acidic side chain + basic side chain. aka SALT BRIDGES
electrostatic attractions
27
happens when two non polar chains are close together
hydrophobic attractions
28
happens between amino acid + polar R groups
hydrogen bonds
29
the strongest of all interactions, groups of two cysteine reaction
Disulfide Bonds
30
The peptide chains in multimeric protiens are called protein ___
subunits
31
Two or more protein aggregate to form large ordered structures
Quaternary protein structure
32
has a heme group, transports oxygen from the lungs to tissue
Hemoglobin
33
oxygen storage molecule in muscles
myoglobin
34
Most abundant protein in all humans (ligaments, bones, skin)
Collagen
35
a protein that contains carbohydrates or carbohydrate derivatives in addition to amino acids
Glycoprotein
35
a protein that contains carbohydrates or carbohydrate derivatives in addition to amino acids
Glycoprotein
36
a conjugated protein that contains lipids in addition to amino acids; help suspend lipids and transport them through the bloodstream
Lipoproteins
37
protective response to the invasion of microorganisms or foreign molecules
Immunoglobulins
38
involved in the transport system for lipids in the bloodstream
Plasma Lipoprotein
39
true or false When it comes to PURPOSE, a fibrous is a functional than a structual
false
40
which is which When it comes to SOLUBILITY, they are generally soluble in water
Globular
41
which is which THey have a repetitive amino acid sequence
Fibrous
42
which is which: they are more sensitive in changes of pH, environment, temperature, etc.
Globular
43
a conjugated protein that contains lipids in addition to amino acids; help suspend lipids and transport them through the bloodstream
Lipoprotein
44
4 types of PLasma Lipoprotein
Very low / Low / High density lipoprotein and Chylomicrons
45
transport dietary triacylglycerols from the intestine to the liver and to adipose tissue.
Chylomicrons
46
transport triacylglycerols synthesized in the liver to adipose tissue
Very-low-density lipoproteins
47
transport cholesterol synthesized in the liver to cells throughout the body
Low-density lipoproteins
48
collect excess cholesterol from body tissues and transport it back to the liver for degradation to bile acids.
High-density lipoproteins