NUR1 200 Lecture Notes - Lecture 3: Protein Biosynthesis, Lysine, Structural Motif
10 May 2016
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Almost always nh3 and coo gr at each end. There are post translation, there is no coo at the end but nh2. Sds binds to and unfold all the proteins. Sds gives all proteins an uniformly negative charge. The native shape of proteins does not matter. Rate of movement will only depend on size: small proteins will move faster, larger proteins will move slower. *this is therefore a method to separate molecules based on their molecular weights; clearly not useful for oligomers because these will be forced apart by the sds. Peptides that may be useful can be obtained by: purification from a natural source, gene biotechnology (isolate gene and clone, direct chemical synthesis. Now possible for molecules up to 100 aa residues in length. Peptide is built up one aa at a time while tethered to a solid support. Key information about a protein can be discovered from the aa sequence.
