Amino Acids, Peptides, Proteins Flashcards
Nonessential Amino Acids
Synthesized in the body **Nonessential SAGAA** of ALAN who likes his mates GLUTs, SPARTA, & ASPARAGus Serine Alanine Glutamate Aspartate Asparagine
Conditionally Essential
Synthesis can be limited under special conditions **Top Cop Places GAG** Tyrosine Cysteine Proline Glycine Arginine Glutamine *Muscular Building Block*
Essential
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
Ketogenic Amino Acids
Converted to acetyl CoA or Acetoacetate
Lesbian Lovers (Lucy & Lisa) on a Keto Diet
Leucine
Lysine
Positively Charged AAs
Love At Home Lysine Arginine Histidine Soluble in H20
Negatively Charged Amino Acids
People usually feel negative about their mates Ass & Glutes
Aspartate
Glutamate
Polar Uncharged R Groups
3 Stone Cold Mean Asparagus Threonine Serine Cysteine Glutamine Asparagine
Nonpolar R groups
All Very Important People Like Good Meth Alanine Valine Isoleucine Proline Leucine Glycine Methionine *Can't form H-bonds with water*
Aromatic R Groups
Trip on TP Tryptophan Tyrosine Phenylalanine *Absorb UV but TRYPTOPHAN absorbs the most*
Both Ketogenic and Glucogenic AA
IP TTT Isoleucine Phenylalanine Tryptophan Tyrosine Threonine
General Structure of AAs
-OOC一αC一H3N+
With an H and R group coming off αC
Amino Acid Forms: L or D?
All natural AAs are in L-form naturally on earth
Can MAKE D-form in lab and on Mars!
Chirality of AAs
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
What AA is the most polar of the non polar group?
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
What are the uncommon amino acids?
Hydroxyproline Hydroxylysine Methyllysine γ-Carboxyglutamate Desmosine Selenocysteine Thyroxine Nmethyl Arginine N-Acetyl Lysine
Modifications of Amino Acids
AA can be phosphorylated, methylated, contain ester etc
These are REVERSIBLE reactions
Amino Acids not found in Proteins
Ornithine
Citrulline
Cause bad breath
Zwitterion
A neutral molecule with a POSITIVE and a NEGATIVE charge.
Difference between amphipathic and zwitterion
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
Titration of AA
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.
Calculating the Isoelectric Point (pI)
pI= .5(pK1 + pK2)
pK1 is the pKa of the positive form
pK2 is the pKa of the negative form
Isoelectric Point (pI)
The pH where the predominant form of the AA is the zwitterion state (aka the net charge is 0!)
Peptides
AAs linked together via peptide bonds
Different than proteins based on size.
Approximately 0-50 AAs
Proteins
One or more polypeptides (chains of AAs linked via peptide bonds)
Peptide Bonds
Carboxylic Acid + Amine Group –> O=C一N一C一R + H20
NON ROTATABLE on the bond C一N
Protein Structure
Primary Structure (linear sequence of AAs) Secondary Structure (αhelix or βsheet) Tertiary Structure (Folding of several αhelix/βsheets) Quaternary Structure (2 or more units)
α Helix
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
β Sheets
Can be parallel (all C-terminus on same side)
Can be Anti-parallel (alternate C-term/N-term)
H-bonds between each sheet
Plasma Proteins
Production of most plasma proteins takes place in liver
EXCEPT IMMUNOGLOBINS - produced by plasma cells
Protein Denaturation & Renaturation
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
Collagen Structure
Quaternary
Positively and Negatively Charged AA in the Body
Should not have a charge