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Department
Biochemistry
Course
Biochemistry 2288A
Professor
Derek Mc Lachlin
Semester
Fall

Description
TEXTBOOK PAGES topic pages introduction 1-6, 11-22, 26-35 1. central dogma 72-73 2. amino acids 121-140 3. protein structure 120, 138-143 3. protein function 89-92, 99-103, 5. enzyme catalysis 140-143, 146-148, 152-153 6. protein purification 164-167 peptide bonds: covalent linkage between two adjacent amino acid molecules > creates a chain - a polypeptide peptide bonds formed through a condensation reaction (dehydration reaction) the residue is the remainder of the molecule (amino acid) after the condensation reaction (dehydration reaction) a polypeptide always has a carboxyl group at one end and an amino group at the other > chain is always written with the amino or N terminus facing left and carboxyl or C terminus facing right results in a protein with structural polarity AMINO ACIDS > or 'alpha amino acid' there are around 500 amino acids but only 20 alpha amino acids > where both the carboxyl and amino groups are attached to the alpha carbon basic structure - 19 of the 20 amino acids have this structure only proline differs - has an NH2+ instead of NH3+ amino group > because precursor is an imino acid with a C=NH group what is its significance? amino acids are chiral - stereoisomers are possible > with the exception of glycine only the L form is incorporated into proteins > although D forms do exist in bacterial cell walls and in some anti
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