[RECALLS] Prelims - 2nd Evals Flashcards
Aromatic amino acid with positive charge:
Histidine
Backbone of cysteine:
Serine
More than 10 residues:
Fibrous
Optically active B carbon:
Isoleucine
Essential for baby even though the body already produces it:
Arginine
Amino acid nucleus:
A-carbon
Rod like appearance:
Alpha helix
Coiled:
Alpha helix
Katong sa UV
Tryptophan
Cyclic
Proline
No L or D isomers:
Glycine
Represents an obligatory interruption of a helix:
Prolyl residue
Katong sa turns/folds:
Turns and bends
Secondary structure:
Hydrogen bonds
2 or more chains are united:
Quarternary
Transforms ammonium ion into a-amino nitrogen:
Aminotransferase
pKa:
Strengths of weak acid
pH>pI
Net charge is negative
Three dimensional shape
Tertiary structure
Temporary fluctuating dipoles:
Van der waals
Pyruvate to alanine
ALT (Alanine transaminase)
3rd reaction (phosphoglycerate to serine)
Dephosphorylation (Oxidation, transamination, dephosphorylation)
Reaction II of tyrosine
Dihydrobiopterin to TETRAHYDROBIOPTERIN (Tyrosine reaction is irreversible)
*Reaction 1: L-phenylalanine to L-tyrosine by phenylalaline hydroxylase
Most hydrophobic
Methionine
Katong secondary structure na naay slant:
Beta parallel
Product sa choline:
Betainealdehyde
Urea cycle precursor:
Ornithine
How many isoforms is formed in a chimeral structure:
2
Double ring daw na amino acid:
Tryptophan
Will facilitate the folding of unfolded structure:
Domains or region
If facilitate refolding process: Contacts and Region
2 amino acids that interrupt in folding:
Proline: Large
Glycine: Small
Angle between alpha carbon and carbonyl carbon:
psi -47
PHIN -57: Alpha carbon and nitrogen carbon
Amino acid not a product in TCA:
Cysteine, Hydroxylysine, Tyrosine ??
Indole
Tyrosine
At physiologic pH:
Zero
When both sides are ionized, capable of binding to a proton:
Zwitterion
Every AA has a pH with no net charge caled pI or isoelectric point so aspartic acid = pi3
Zero
Ratio greater than 10
Fibrous proteins: structural proteins like HAIR, FIBRIN, COLLAGEN
Sequence of amino acids in a polypeptide chain:
Primary structure
Spacing of a complete turn of amino acid residue:
3.6 Aminoacyl residue per turn
The H+ bonds are evenly placed, equidistant but slant in alternate direction
Paralle betapleated sheet
Presence of this amino acid represents an obligatory interruption of a helix which creates a bend
Proyly residue
The whole chain folds itself into its final 3D shape:
Tertiary structure proteins
Temporary fluctuating dipoles in one of these groups could induce opposite dipoles in another group on a nearby folded chain
Van der waals dispersion forces
Unfolded proteins that retain a number of secondary structures that facilitate the refolding process
Contacts and regions
Most transaminases generate:
GLU & ASP
Provide proteins with unique structural and functional properties
R-groups
Amino acids are colorless except for:
FWY
Present in multiple tandem repeats:
Proline
Least hydrophobic, nonpolar, aromatic a.a side chain
Tyrosine
Most hydrophobic, nonpolar, aromatic a.a side chain:
Phenylalanine
Arginine:
Guanidino group
Imidazole functional group (Has 2 N atoms in a 5 membered unsaturated ring)
Histidine
Decrease in L-dopa:
Parkinson’s disease
