Amino Acids and Peptides Flashcards

(53 cards)

1
Q

What is the 21st amino acid?

A

Selenocysteine

(that include certain peroxidases and reductases, selenoprotein P1, and the iodothyronine deiodinase responsible for converting the prohormone thyroxine(t4) and t3.

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2
Q

The alpha carbon of every amino acid is chiral except

A

GLYCINE

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3
Q

All protein amino acids all share the absolute configuration of L- glyceraldehyde and thus are defined as L- amino acids. TRUE OR FALSE

A

True

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4
Q

Provide monomer units for formation of long polypeptide chains of proteins

A

L-amino acids and their derivatives

Cellular fxns:
Nerve transmission
Biosynthesis of porphyrins, purines, pyrimidines, urea

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5
Q

Cellular fxns of L amino acid

A

Nerve transmissions

Biosynthesis of porphyrins, purines, pyrimidines, urea

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6
Q

Short polymers of amino acids

A

Peptides

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7
Q

Perform roles in neuroendocrine system

A

Peptides

.. Such as hormones, hormone-releasing factors, neuromedulators, neurotransmitters

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8
Q

Only L-amino acids occur in Proteins. TRUE OR FALSE

A

TRUE

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9
Q

Amino acids may have positive or negative charge. TRUE OR FALSE

A

TRUE

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10
Q

pKa values express the strengths of strong acids. TRUE OR FALSE.

A

FALSE. Weak acids.

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11
Q

pKa values do not vary w/ the environment. TRUE OR FALSE.

A

False. Do vary.

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12
Q

At its isoelectric pH (pI), an amino acid bears no net charge. TRUE OR FALSE

A

True

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13
Q

The solubility of Amino Acids reflects their ionic character. TRUE OR FALSE.

A

TRUE

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14
Q

A given amino acid having more than one triplet coding for it.

A

Redundancy. (Limits the available codons to the 20 amino acids)

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15
Q

Humans cannot synthesize 10 of the 20 common L-amino acids. TRUE OR FALSE

A

TRUE. Thus, human diet must contain adequate quantities of these essential amino acids

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16
Q

Nutritionally essential Amino Acids

A

HILLAMPTTV

Histidine
Isoleucine
Leucine
Lysine
Arginine
Methionine
Phenylalanine
Threonine
Tryptophan
Valine
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17
Q

Found in peroxidases and reductase where it participates in the catalysis of electron transfer reactions.

A

Selenocysteine

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18
Q

Not specified by a simple three letter codon unlike the others

A

Selenocysteine

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19
Q

A selenium ion replaces ______ of its structural analog, cysteine.

A

Sulfur

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20
Q

All proteins/amino acids all share the L-glyceraldehyde configuration. TRUE OR FALSE

A

TRUE. thus are L-amino acids.

Some proteins/amino acids are dextrorotatory/ levorotatory.

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21
Q

Amino acids that fulfill roles in metabolic processes

A

OCA - urea synthesis

Ornithine
Citrulline
Argininosuccinate

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22
Q

Other metabolic processes

A

Tyrosine in thyroid hormone
Glutamate in neurotransmitter
Biosynthesis

23
Q

Both -COOH and R-NH3 are strong acids. True or false

A

False. Weak acids.

24
Q

Molecules that contain an equal number of ionizable groups of opposite charge and therefore bear NO NET CHARGE (electrically neutral)

25
At its isoelectric ph (pI), an amino acid bears no net charge. TRUE OR FALSE
True
26
Isoelectric pH
pI - the pH midway between pKa values on either side of the isoelectric species - zwitterions are examples of isoelectric species
27
Net charge depends upon
1) pKa values of its functional groups | 2) pH of its surrounding medium
28
Characteristic pH at which the net electric charge is zero is called
Isoelectric point or "pI"
29
Amino acid at the isoelectric pI is called
Zwitter ion - electrically neutral ( not migrating in an electrical field)
30
Polar environment favors _____ form.
Charged form. | Polar- charged form (Non polar - uncharged form)
31
Non polar environment: A) raises the PKa of a _____ group. B) lowers pKa of ____ group.
A) carboxyl group (making it weaker acid) | B) amino group (making it a stronger acid)
32
Charged functional groups of AA ensure that they are: ________ in polar solvents (ex. ___ and ____) ________ in nonpolar solvents (___, ____, ____)
Soluble ( water and ethanol) | Insoluble (benzene, ether, hexane) BEH
33
Can reinforce/counteract solvent effects
Adjacent charged groups
34
Amino acids do not absorb light and thus are colorless. True or false.
True
35
Ten times more efficient in absorbing light than phenylalanin and tyrosine. Major contributor of protins to absorb light
TRYPTOPHAN (250-290nm)
36
Hydrophobic R groups of alanine, valine, leucine and isoleucine occur primarily in the + AROMATIC R groups of phenylalaninr , tyrosine and tryptophan
Interior of cytosolic proteins
37
Smallest amino acid, often occurs where peptides bend sharply
Glycine
38
Stabilize specific protein conformations via ionic interactions or salt bridges
Charged R groups of basic and acidic amino acids
39
Histidine
Plays unique roles in enzymatic catalysis
40
Plays a role in ezymatic catalysis
Histidine Pka of its imidazole proton permits it to fxn at neutral ph as either a base or acid
41
Most important reaction of amino acids
Formation of peptide bond
42
Chemical reactions exhibit all of its characteristic chemical rxns
- carboxylic acid group (formation of esters, amides, acid anhydrides) - amino groups: acylation, amidation, esterification
43
Alcohol group of SERINE and the primary thioalcohol group of cysteine are excellent
NUCLEOPHILES
44
Amino acid sequence determines primary structure. True or False
TRUE
45
Peptide bond has
Partial Double bond character
46
Peptides are
Polyelectrolytes
47
Noncovalent forces constrain
Peptide conformations
48
Amino acids present in peptides are called
Aminoacyl residues
49
Peptide hormones typically contain ONLY the a-amino acids of proteins. TRUE OR FALSE
True. Other peptides contain non protein amino acids or amino acids linked by ATYPICAL PEPTIDE BOND ex. Glutathione
50
Formation of peptides from amino acid is therefore accompanied by a net loss of one positive and one negative charge per peptide bond formed.
TRUE
51
The physiologically active conformation reflects the collective contributions of the
Amino acid sequence Steric hindrance Non covalent interactions
52
Widely used for detecting amino acids, forms a purple product w/ amino acids and a yellow adduct with imine groups of proline and hydroxyproline
NINHYDRIN
53
Some proteins contain additional amino acids that arise by
Post- translational modification of an amino acid present in the peptide