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1st Term > BIOCHEM PROTEINS > Flashcards

BIOCHEM PROTEINS Flashcards

1
Q

natural product containing nitrogen

A

protein

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2
Q

“proteios”

A

of first importance”

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3
Q

naturally occurring unbranched polymers that contains building blocks of AMINO ACIDS

A

protein

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4
Q

the amino acids in a protein is connected by a?

A

peptide bonds

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5
Q

the structure of a protein is known as

A

native conformation

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6
Q

protein refer to its 3D structure with biological function

A

native conformation

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7
Q

it is the changes in a protein’s native conformation.

A

denaturation

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8
Q

it is a compound containing a carboxyl group and amino group

A

Amino Acids

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9
Q

there are only ___ amino acids found in a human, known as the?

A

20, Standard Amino Acids

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10
Q

Standard Amino Acids are __-amino acids.

A

a-amino acids

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11
Q

a standard amino acid are a-amino acids because they have a?

A

carbonyl group and primary group

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12
Q

the most abundant enantiomer of amino acid?

A

L-amino acid

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13
Q

to represent the D and L enantiomers of the Standard Amino Acids, we use the?

A

Fischer projection

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14
Q

What standard amino acids are found in nature and in proteins?

A

L isomers

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15
Q

a structure with monoamino monocarboxylic acid with non- polar side chain

A

non-polar

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16
Q

it has a hydrophobic chemical characteristics of side chain

A

non-polar

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17
Q

it has a structure of a monoamino monocarboxylic acid with polar side chain

A

neutral polar

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18
Q

it does not ionize at near pH 7 chemical characteristic of a side chain

A

neutral polar

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19
Q

it has a structure of monoamino-dicarboxylic acid

A

acidic polar

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20
Q

it has negative charge near ph7 due to the deprotonation of the carbonxyl group in the side chain chemical characteristic side chain

A

acidic polar

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21
Q

it has a structure of diamino monocarboxylic acid

A

basic polar

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22
Q

it has a postive charge near ph7 due to the protonation of the amino group in the side chain chemical characteristic of side chain

A

basic polar

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23
Q

contains hydrocarbons

A

non-polar amino acid

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24
Q

contains alcohol, phenol, thiol and amide

A

polar-neutral amino acids

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25
contains extra amino group
polar basic
26
donates hydrogen; contains extra carbonyl
polar acidic amino acids
27
standard amino acids that the human body cannot adequately synthesize and must be OBTAINED FROOM DIETARY SOURCES.
PVT TIM HALL
28
only essential for infants normal growth, but becomes nonessential amino acid as they grow into adulthood
arginine
29
contain adequate amounts of these conditionally essential amino acids
human milk and infant formula milk
30
contains all of the essential amino acids in adequate amounts as the body needs.
complete dietary protein (high-quality protein)
31
does not ontin in adequate amounts, relative to the body's needs
incomplete dietary protein
32
substance that can act as an acid in basic environment and act as a base in an acidic environment
amphoteric substance
33
producing a negatively charged conjugate base known as?
carboxylate
34
producing a positively charged conjugate acid known as?
quaternarnary ammonium ion
35
the -COOH (carboxyl group) of the standard amino acid is ___ while the -NH2 (amino acid) is __
deprotonated or losing; protonated (accepted)
36
a molecule having a positive charge on one side and negative charge on the other
zwitterion or dipolar ion
37
a chain of amino acids that is formed when the carboxyl group of the a-carbon of an amino acid reacts with the amino group of the second amino acid.
peptide
38
what type of reaction is the formation of peptide?
dehydration reaction
39
what is the product after the dehydration reaction?
water
40
in a peptide chain, this contains the amino group.
n-terminal
41
in a peptide chain, this contains the free carboxyl group
c-terminal
42
each hormone is a?
nonapeptide
43
pentapeptide neurotransmitters produced by the brain itself
enkephalins
44
it is a tripeptide with the sequence Glu-Cys-Gly and serves as an antioxidant
glutathione
45
contain ONLY ONE POLYPEPTIDE CHAIN (protein subunit)
Monomeric Proteins
46
contain mORE THAN ONE PROTEIN SUBUNITS
multimeric proteins
47
only amino acid is present
simple proteins
48
contain amino acids and prosthetic groups
conjugated proteins
49
denotes the number, kind and sequence of amino acids in protein
primary structure
50
a helical (spiral) repeating structure of a polypeptide chain
a-helix
51
one turn of the helix comprises ___ amino acid residues
3.6
52
the linear distance between corresponding points on successive turns are called
pitch
53
a helix breaker
proline
54
creates bend in the backbone
proline
55
causes crowding which result to steric repulsion
presence of bulky groups
56
peptide backbone is almost fully extended
b-pleated sheets
57
the over-all three dimensional arrangement of all the atoms in a protein
tertiary structure
58
2 types of shapes in tertiary structure of a protein
globular sand fibrous shape
59
provides a covalent linkage that binds together the two chains or the two parts of the same chain (2 cysteine far away from each other)
disulfide bond
60
this interaction can occur between POLAR NEUTRAL (except cysteine)
side-chain hydrogen bonding
61
2 amino residues with ionized side chains. (oppositely charged group)
electrostatic attraction (salt bridge)
62
polar groups outward and non-polar groups inward (non-polar groups); weakest interaction.
hydrophobic interaction
63
two side chains with the same charge would normally repel each other but they can also be linked via metal ions (2 polar acids with metal in between)
meral ion coordination
64
What ate the non polar amino acids?
Leucine (Leu, L) Proline (Pro,P) Alanine (Ala, A) Valine (Val, A) Methionine (Met, M) Tryptophan (Tyr, W) Phenylalanine (Phe, F) Isoleucine (Iso, I)
65
a structure of protein that pertains only to multimeric proteins
Quaternary structure
66
The chains may be identical or different. Commonly examples are dimers, trimers, tetramers consisting of two-four polypeptide chains.
Quaternary structure
67
Subtle changes in structure at one site on a protein molecule may cause drastic changes in properties
Allosteric proteins
68
Means that when one oxygen molecule is bound, it becomes easier for the next molecule to bind.
Positive cooperativity
69
The oxygen binding curve of myoglobin
Hyperbolic
70
The oxygen binding curve of hemoglobin
Sigmoidal
71
Peptides that contain the same kind and number of amino acids but differ in order are called
Isomeric peptides
72
disruption of peptide bonds causing liberation of free amino acids
Hydrolisis
73
Can be carried out in the presence of strong acids, strong bases and enzymes
Hydrolisis
74
causes disruption or unfolding of proteins
Denaturation
75
Causes loss of biological activity
Denaturation
76
Can be reversible or irreversible
Denaturation
77
Results in coagulation and precipitation
Denaturation
78
Cleaves hydrogen bonds
Heat
79
Can change protein conformation by opening up the hydrophobic regions
Detergents or Surface active agents
80
Affects both salt bridges and hydrogen bonds
Acids, based and salts
81
1. Can break disulfide bonds 2. Latter effect 3. Make up human hair, contains high percentage of DISULFIDE BONDS
Reducing agents, such as 2-mercapoethanol
82
Reverses the preceding reaction, forming nee disulfide bonds, which now hold the molecules together in the desired positins
Oxidizing agent

1st Term (15 decks)

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