Amino Acids, Peptides, Proteins Flashcards

1
Q

Nonessential Amino Acids

A
Synthesized in the body
**Nonessential SAGAA** of ALAN who likes his mates GLUTs, SPARTA, & ASPARAGus
Serine
Alanine
Glutamate
Aspartate
Asparagine
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2
Q

Conditionally Essential

A
Synthesis can be limited under special conditions
**Top Cop Places GAG** 
Tyrosine
Cysteine
Proline
Glycine
Arginine
Glutamine *Muscular Building Block*
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3
Q

Essential

A
Cannot be synthesized by our bodies
**Essential PVT TIM HaLL
Phenylalanine
Valine
Threonine (three)
Tryptophan (trip over Tim)
Isoleucine
Methionine
Histidine
Leucine *Muscular Building Block*
Lysine
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4
Q

Ketogenic Amino Acids

A

Converted to acetyl CoA or Acetoacetate
Lesbian Lovers (Lucy & Lisa) on a Keto Diet
Leucine
Lysine

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5
Q

Positively Charged AAs

A
Love At Home 
Lysine
Arginine
Histidine
Soluble in H20
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6
Q

Negatively Charged Amino Acids

A

People usually feel negative about their mates Ass & Glutes
Aspartate
Glutamate

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7
Q

Polar Uncharged R Groups

A
3 Stone Cold Mean Asparagus
Threonine
Serine
Cysteine
Glutamine
Asparagine
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8
Q

Nonpolar R groups

A
All Very Important People Like Good Meth
Alanine
Valine
Isoleucine
Proline
Leucine
Glycine
Methionine
*Can't form H-bonds with water*
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9
Q

Aromatic R Groups

A
Trip on TP 
Tryptophan
Tyrosine
Phenylalanine
*Absorb UV but TRYPTOPHAN absorbs the most*
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10
Q

Both Ketogenic and Glucogenic AA

A
IP TTT
Isoleucine
Phenylalanine
Tryptophan
Tyrosine
Threonine
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11
Q

General Structure of AAs

A

-OOC一αC一H3N+

With an H and R group coming off αC

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12
Q

Amino Acid Forms: L or D?

A

All natural AAs are in L-form naturally on earth

Can MAKE D-form in lab and on Mars!

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13
Q

Chirality of AAs

A

GLYCINE is the only AA that is not Chiral (2 H groups)
Can form non-superimposable mirror images of each other
(L and D forms) which are enantiomers

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14
Q

What AA is the most polar of the non polar group?

A

Alanine, Valine, Isoleucine, Proline, Leucine, Glycine, Methionine are all non polar. Glycine and Alanine are the “least” non polar because they have the smallest R groups.
More alkyl groups on R, the more non polar the AA will be

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15
Q

What are the uncommon amino acids?

A
Hydroxyproline
Hydroxylysine
Methyllysine
γ-Carboxyglutamate
Desmosine
Selenocysteine
Thyroxine 
Nmethyl Arginine
N-Acetyl Lysine
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16
Q

Modifications of Amino Acids

A

AA can be phosphorylated, methylated, contain ester etc

These are REVERSIBLE reactions

17
Q

Amino Acids not found in Proteins

A

Ornithine
Citrulline
Cause bad breath

18
Q

Zwitterion

A

A neutral molecule with a POSITIVE and a NEGATIVE charge.

19
Q

Difference between amphipathic and zwitterion

A

Amphipathic: can only have ONE charge (- charge and non polar chain or + charge and polar chain)
Zwitterion: TWO charges in the same molecule for a net charge of 0

20
Q

Titration of AA

A

Have two buffer regions because it can lose two H+.
Goes from + charge 一> neutral (zwitterion) 一> - charge
pI is when zwitterion is the most predominant form and it precipitates out of solution.

21
Q

Calculating the Isoelectric Point (pI)

A

pI= .5(pK1 + pK2)
pK1 is the pKa of the positive form
pK2 is the pKa of the negative form

22
Q

Isoelectric Point (pI)

A

The pH where the predominant form of the AA is the zwitterion state (aka the net charge is 0!)

23
Q

Peptides

A

AAs linked together via peptide bonds
Different than proteins based on size.
Approximately 0-50 AAs

24
Q

Proteins

A

One or more polypeptides (chains of AAs linked via peptide bonds)

25
Q

Peptide Bonds

A

Carboxylic Acid + Amine Group –> O=C一N一C一R + H20

NON ROTATABLE on the bond C一N

26
Q

Protein Structure

A
Primary Structure (linear sequence of AAs)
Secondary Structure (αhelix or βsheet)
Tertiary Structure (Folding of several αhelix/βsheets)
Quaternary Structure (2 or more units)
27
Q

α Helix

A

There are approximately 3.6 residues/turn (5.4nm)
Hydrogen bonds are formed along the spine
*Similar to DNA (outside hydrophilic inside phobic)
Proline is most likely AA to disrupt the αHelix

28
Q

β Sheets

A

Can be parallel (all C-terminus on same side)
Can be Anti-parallel (alternate C-term/N-term)
H-bonds between each sheet

29
Q

Plasma Proteins

A

Production of most plasma proteins takes place in liver

EXCEPT IMMUNOGLOBINS - produced by plasma cells

30
Q

Protein Denaturation & Renaturation

A

Start in NATIVE state
Add Urea and Mercaptoethanol
Protein unfolds, disulfide cross-links reduced (broken)
LOSES 2/3 STRUCTURE, BUT NOT PRIMARY
Remove Urea and Mercaptoethanol
Back to Native, disulfide cross-links correctly reformed

31
Q

Collagen Structure

A

Quaternary

32
Q

Positively and Negatively Charged AA in the Body

A

Should not have a charge