What factors can change the pKa value of an amino acid residue, and in which direction?
How does hplc differ from normal column chromatography, and what are its advantages?
How are free energy changes related to enthalpy changes and entropy changes?
Why are right-handed helices more stable than left-handed helices?
How are reaction rates dependent upon free energy changes?
Why are free cysteines treated with iodoacetate prior to protein sequencing?
How are free energy, equilibrium and spontaneity related to each other?
Where do hydrophobic and hydrophilic residues usually end up after protein folding?
What are the structures of the products of this reaction, and how are they identified?
How does a random coil differ from an irregularly structured region?
What are hydrophobicity scales, and how are they used?
How are coupled reactions used in biochemistry?
What type of column is generally used to separate amino acids from each other?
Why is the t-butyloxycarbonyl protecting group such a good choice for amino acid synthesis?
How much empty space is found in globular proteins?