Chemistry and Metabolism of Amino Acids Flashcards
General Structure of Alpha Amino Acid
acid (carboxyl group)
basic (amino group)
r group (distinct side chain)
Non-alpha AA present in tissues in free form
Beta alanine
Beta aminoisobutyrate
gamma aminoisobutyrate
Amino acid that is an IMINO ACID
Proline
Simple Amino Acid
Glycine
Alanine
Branched Chain AA
LIV
Lysine
Isoleucine
Valine
Sulfur Containing AA
Cysteine
Methionine
Hydroxyl Containing AA
Serine
Threonine
Tyrosine
AA w/ Amide Group
Asparagine
Glutamine
Acidic Amino Acid
Aspartate
Glutamate
Basic Amino Acid
Arginine - MOST BASIC
Lysine
Histidine
Aromatic AA
Histidine
Phenyalanine
Tyrosine - w/ OH group
Tryptophan
With heterocyclic Aromatic Ring
Tryptophan
Histidine - basic AA
Disrupts the alpha helix structure of proteins
PG
Proline
Glycine
SMALLEST SIDE CHAIN
Glycine
LARGEST SIDE CHAIN
Tryptophan
MOST BASIC AA
Arginine
MOST ACIDIC AA
Aspartic Acid
Known as the 21st AA
SELENOCYSTEINE
Known as the 22nd AA (found in Archaea)
PYRROLYSINE
PURELY KETOGENIC AA
LEUCINE
BOTH Ketogenic and Glucogenic
Phenylalanine Isoleucine Tyrosine Tryptophan Lysine - predominantly ketogenic
AA which absorb 250-290 nm UV light
Tryptophan
Phenylalanine
Tyrosine
Formed from cytosine and uracil
Beta-Alanine
MC amino acid that undergo oxidative deamination
Glutamic Acid (Glutamate)
General test for proteins
Cupric ions in alkaline medium forms VIOLET color w/ peptide bond nitrogen
BIURET TEST - needs a minimum of 2 peptide bonds
dipeptides and individual AA - do not answer biuret test
General test for all alpha amino acids
Ninhydrin Test
AA + 2 mols of Ninhydrin –> aldehyde w/ 1 carbon atom less + CO2 + Purple Complex (Ruhemann’s purple)
AA which do NOT give purple color
Proline and Hydroxyproline - YELLOW
Glutamine and Asparagine - BROWN
Determined by the AA sequence of protein
Primary Structure
N terminus to C terminus
The ONLY structure preserved in denaturation
Primary Structure
Folding of SEGMENTS of polypeptides
Stabilized by hydrogen bonds
Secondary Structure
alpha helix
beta sheets
Alpha helix
Keratin
Hemoglobin
Beta sheets
Amyloid
Immunoglobulins
Overall 3D structure of of proteins
Stabilized by disulfide bonds, hydrophobic interactions, hydrogen bonds and ionic interactions
Tertiary Structure
Interaction of atleast 2 peptide chains (tertiary structure)
Quaternary Structure