BIOL 200 Final: BIOL 200 Exam.pdf
5 Aug 2012
School
Department
Course
Professor
Document Summary
Amino acids: can be dexter or laevus (d or l) isomers (enantiomers) with a central alpha carbon. Amino acids differ by their r functional groups. Cysteine has a sulfhydryl group (-sh) that can form disulphide bonds (s-s) with another cysteine. This creates intra and inter cross-linking that stabilize folded structure. Proline has a rigid ring structure that can create kinks or make bulges that disrupt structure. Glycine has a symmetrical r group (r group is a hydrogen). Protein function is derived from the three- dimensional structure, and the three- dimensional structure is specified by the amino-acid sequence. The three-dimensional structure is also known as the protein"s conformation. Primary (sequence) -> secondary(local folding) -> tertiary (long range folding) -> Tertiary, quaternary and supramolecular all form a functional protein. These functions include: regulation (on and off), structure (microtubules), movement, catalysis (enzymatic proteins), transport, and signaling: not all proteins form a quaternary structure because some do not consist of subunits.
