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Biochemistry Lecture > Proteins > Flashcards

Proteins Flashcards

1
Q

Made up of amino acids that are joined together by ___

A

Peptide bonds

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2
Q

There are __ naturally occurring amino acids

A

20

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3
Q

Most genetic information directs the synthesis of protein

A

Central Dogma

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4
Q

__ properties of amino acids that play an important role in their ___

A

Chemical , Function

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5
Q

8 Functions of Proteins

A 
Structure
Catalysts
Movement
Transport
Hormones
Protection
Storage 
Regulation
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6
Q

Protein function that is constituent of the skin, bone and hair

A

Structure – Keratin and collagen

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7
Q

2 properties of collagen and keratin that is attributed to their role

A

Fibrous – Hydrophobic

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8
Q

Protein function that hastens all reactions in the living system

A

Catalyst

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9
Q

Protein that hastens all metabolic reactions

A

Enzymes

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10
Q

Example of roles of enzyme in the body

A

Conversion of Alcohol by alcohol dehydrogenase
Digestion of carbs by salivary amylase
For blood clotting
Muscle contraction

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11
Q

Protein Function governed by muscle proteins

A

Movement – Myosibn and Actin filaments

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12
Q

Protein function chiefly done by hemoglobin

A

Transport

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13
Q

Protein function done by fibrinogen and antibodies

A

protection

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14
Q

Protein function with examples of insulin, oxytocin, and human growth hormone

A

Hormones

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15
Q

Protein function with examples of Casein, ovalbumin and ferritin

A

Storage

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16
Q

Protein function storage (Analogy)
Casein : ___
Ovalbumin : ____
Ferritin : ____

A

Casein : milk
Ovalbumin : eggs and nutrients of newborn
Ferritin : Iron

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17
Q

Protein Function that controls when the expression of genes should take place

A

Regulation

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18
Q

2 Types of proteins

A

Globular and Fibrous proteins

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19
Q

Predominant type of protein

A

Globular protein

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20
Q

type of protein for structural purposes

A

fibrous protein

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21
Q

type of protein that have a characteristic of elongated wires

A

Fibrous proteins

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22
Q

type of protein that is insoluble in water and have high percentage of secondary structure – alpha helix and beta pleated sheets

A

Fibrous protein

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23
Q

Type of protein that is the vast majority of all known enzymes

A

Globular protein

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24
Q

Predominant type of protein

A

globular protein

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25
Type of protein that forms colloid with water
globular protein
26
type of of protein that is spherical in shape
globular protein
27
Building blocks /monomer unit of protein
amino acid
28
Compound that contains both the amino group and carboxyl group
amino acid
29
An amino acid in which the amino group is on the carbon adjacent to the carboxyl group
Alpha amino acid
30
Alpha amino acids are commonly written in their ___ form
unionized form
31
Amino acids' internal salt form
zwitterion
32
a form of an amino acid with the presence of charged group (positive - amino group ; negative - carboxyl group)
zwitterion
33
form of an amino acid that results to net charge of 0
zwitterion
34
All amino acids have at least one stereocenter and are chiral except for
Glycine (Gly, G)
35
Vast majority of amino acids have this kind of configuration
L-configuration
36
2 types of configuration at the alpha carbon
L-configuration | D-configuration
37
Examples of D-configuration proteins
sugars and carbs
38
type of configuration that is prevalent in nature
L-configuration
39
Amino acids that are nonpolar (hydrophobic)
``` Alanine (Ala, A) Glycine (Gly, G) Valine (Val, V) Isoleucine (Ile, I) Leucine (Leu, L) Methionine (Met, M) Phenylalanine (Phe, F) Proline (Pro, P) Tryptophan (Trp, W) ```
40
Alanine (Ala , A) Side chain
Aliphatic (Hydrocarbon) side chain
41
Glycine (Gly, G) side chain
No stereocenter ; not chiral
42
Valine (Val, V) side chain
Aliphatic (hydrocarbon) side chain
43
Isoleucine (Ile, I) side chain
Aliphatic (hydrocarbon) side chain | isomer of isoleucine
44
Leucine (Leu, L) side chain
Aliphatic (hydrocarbon) side chain
45
Methionine (Met, M) side chain
Aliphatic (hydrocarbon) side chain | Additional Sulfur
46
Phenylalanine (Phe, F) side chain
Aromatic Ring side chain
47
Proline (Pro, P) side chain
Imino acid becaue of Secondary amino group
48
Tryptophan (Trp, W) side chain
Indole Ring (2 aromatic rings)
49
Amino acids with Polar and neutral / uncharged side chains
``` Asparagine (Asn, N) Glutamine (Gln, Q) Tyrosine (Tyr, T) Threonine (Thr, R) Serine (Ser, S) Cysteine (Cys, C) ```
50
Asparagine (Asn, N) side chain
aliphatic hydrocarbon and amide side chain
51
Glutamine (Gln, Q) side chain
aliphatic hydrocarbon and amide side chain
52
Tyrosine (Tyr, Y) side chain
aromatic ring and hydroxyl group side chain
53
Threonine (Thr, R)
Aliphatic hydrocarbon and hydroxyl group side chain
54
Serine (Ser, S) side chain
Aliphatic hydrocarbon and hydroxyl group side chain
55
Cysteine (Cys, C)
Aliphatic hydrocarbon and thiol / sulfihydryl group side chain)
56
Amino acids with acidic and charged side chains
``` Aspartic Acid (Asp, D) Glutamic acid (Glu, E) ```
57
Aspartic acid (asp, D) side chain
Aliphatic hydrocarbon and additional carboxyl group side chain
58
Glutamic acid (Glu, E) side chain
Aliphatic hydrocarbon and additional carboxyl group side chain
59
Amino acids with basic and charged side chains
Arginine (Arg, R) Histidine (His, H) Lysine (Lys, K)
60
Arginine (Arg, R) side chain
Aliphatic hydrocarbon and guanidino with additional amino group side chain
61
Histidine (His, H) side chain
Aliphatic hydrocarbon and aromatic ring and additional amino group
62
Lysine (Lys, K) side chain
Aliphatic hydrocarbon and additional amino group
63
Ability to rotate on its plane
Chirality of the Carbon
64
If we add a strong base such as NaOH to the solution and bring its pH to 14
a proton is transferred FROM the NH3+ making it a negative ion
65
If we add a strong acid such as HCl to bring the pH of the solution to 0.0
it denotes a proton TO the COO- making it a Positive Ion
66
The pH at which majority of the molecules of a compound in a solution has no net charge
Isoelectric point
67
Isoelectric point has how many charge
0
68
Formula of Isoelectric point (pI)
(Pk1+Pk2) / 2
69
Amino acid that is easily oxidized
Cyteine convertine -SH group to S-S disulfide | From Cysteine to Cystine
70
Amino acids that are used in protein of BRAIN TRANSMITTERS
Phenylalanine, Tryptophan, Tyrosine
71
Amino acids that undergo Hydroxylation (oxidation)
Proline - hydroxyproline Lysine - hydroxylysine Cysteine - cystine
72
Amino acids that undergo Iodination
Tyrosine - Thyroxine
73
AMIDE BOND between the alpha carboxyl group of an amino acid and amino group of another amino acid
Peptide bond
74
At physiological pH (7.4) the carboxyl group is ____, the amino group is ____ so an isolated amino acid would bear both a positive and negative charge
carboxyl group - Unprotonated | amino group - protonated
75
the different structure and function of amino acids are attributed by its
R-group
76
A short polymer of amino acids joined by peptide bonds; they are classified by the number of amino acids in the chain
peptide
77
a molecule containing two amino acids joined by a peptide bond
Dipeptide
78
a molecule containing three amino acids joined by peptide bonds
Tripeptide
79
a macromolecule containing many amino acids joined by peptide bonds
Polypeptide
80
a biological macromolecule containing at least 30-50 AMINO ACIDS joined by peptide bonds
Protein
81
individual amino acid units are referred to as
Residues
82
Formula of number of amino acid residues
number of amino acids - 1
83
A peptide bond is typically written as
carbonyl group bonded to an N-H group
84
There is about __% double bond character to the C-N bond of a peptide bond
40%
85
Peptide bond between two amino acid shows what kind of structure
PLANAR
86
the amino acid at the end of the chain having the free -COO- group
C-terminal amino acid
87
the amino acid at the end of the chain having the free -NH3+ group
N-terminal amino acid
88
At a pH above (more basic than) its pI it has a net charge of
NEGATIVE NET CHARGE
89
At a pH below (more acidic than) its pI it has a net charge of
POSITIVE NET CHARGE
90
Proteins are ____ in water at their isoelectric points A. More soluble B. Least soluble
B. Least soluble / Insoluble
91
Proteins at their isoelectric points can be __ from solution
precipitated meaning it can easily be separated since they are insoluble at this point
92
Amino acids are ___ and they can exist as ___
Stereoisomers ; Enantiomer

Biochemistry Lecture (8 decks)

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