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Biochemistry > Protein > Flashcards

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
Q

4 Interactions Responsible for Tertiary Structure

A
  1. covalent disulfide bonds,
  2. electrostatic attractions (salt
    bridges),
  3. hydrogen bonds, and
  4. hydrophobic attractions
26
Q

involves acidic side chain + basic side chain. aka SALT BRIDGES

A

electrostatic attractions

27
Q

happens when two non polar chains are close together

A

hydrophobic attractions

28
Q

happens between amino acid + polar R groups

A

hydrogen bonds

29
Q

the strongest of all interactions, groups of two cysteine reaction

A

Disulfide Bonds

30
Q

The peptide chains in multimeric protiens are called protein ___

A

subunits

31
Q

Two or more protein aggregate to form large ordered structures

A

Quaternary protein structure

32
Q

has a heme group, transports oxygen from the lungs to tissue

A

Hemoglobin

33
Q

oxygen storage molecule in muscles

A

myoglobin

34
Q

Most abundant protein in all humans (ligaments, bones, skin)

A

Collagen

35
Q

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

A

Glycoprotein

35
Q

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

A

Glycoprotein

36
Q

a conjugated protein that
contains lipids in addition to
amino acids; help suspend lipids and
transport them through the
bloodstream

A

Lipoproteins

37
Q

protective response to the invasion of
microorganisms or foreign molecules

A

Immunoglobulins

38
Q

involved in the transport system for
lipids in the bloodstream

A

Plasma Lipoprotein

39
Q

true or false

When it comes to PURPOSE, a fibrous is a functional than a structual

A

false

40
Q

which is which

When it comes to SOLUBILITY, they are generally soluble in water

A

Globular

41
Q

which is which

THey have a repetitive amino acid sequence

A

Fibrous

42
Q

which is which: they are more sensitive in changes of pH, environment, temperature, etc.

A

Globular

43
Q

a conjugated protein that contains lipids in addition to
amino acids; help suspend lipids and transport them through the bloodstream

A

Lipoprotein

44
Q

4 types of PLasma Lipoprotein

A

Very low / Low / High density lipoprotein and Chylomicrons

45
Q

transport dietary
triacylglycerols from
the intestine to the
liver and to adipose
tissue.

A

Chylomicrons

46
Q

transport
triacylglycerols
synthesized in the
liver to adipose
tissue

A

Very-low-density
lipoproteins

47
Q

transport cholesterol
synthesized in the
liver to cells
throughout the
body

A

Low-density
lipoproteins

48
Q

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

A

High-density
lipoproteins

Biochemistry (14 decks)

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