Midterm 2 Random Flashcards
primary structure
what amino acids make up the structure
secondary structure
describes some aspects of 3d, h-bonding between backbone, a-helix (flexible), and beta-pleated sheets (strong)
tertiary structure
how protein folds to achieve active form (side chain int.: h-bonding, salt bridges, hydrophobic effects, disulfide bonds, pi-stacking)
quaternary structure
multiple subunits in active form (bonding motif in center of subunits)
denaturing a protein
-disrupt interactions
-change pH- h-bonding-salt bridge most affected
-chemical: THF disrupts hydrophobic most
-heat + agitation
Peptide bonds
connect the residues
enzymes
catalyze reactions lowers delta G double dagger
pi-stacking
sandwich, t-shaped, parallel-displaced
synthesis of amino acids
Strecker Synthesis:
1) NH3, trace acid
2)HCN
3) acid, D
heterocyclic amino acids
Proline, tryptophan, histidine:
confers a variety of properties, catalysis, and pi-stacking
Benzene Amino Acids
Tyrosine, Phenylalanine:
useful for hydrophobic pockets, pi-stacking, and the creation of complex biomolecules
Amide-based Amino Acids
Asparagine, glutamine
amide in side chain, increases polarity of the compound, can engage in coupling rxns and other synthetic routs
Basic Amino Acids
-amine on their side chains
-+1 charge
-heavily involved in catalysis
-histidine can act as acid or base b/c pKa value
-engages in Acid Catalysis
Acidic Amino acids
-carboxylic acid on side chain
-can engage in basic catalysis
-low pka values, usually in conj. base form increasing water solubility
Sulfur containing Amino acids
-used to create hydrophobic pockets in proteins