Intro to Random Procs - with Applns to Signals and Systems by W. Gardner 2nd ed

By W. Gardner 2nd ed

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1987). Differential racemization of aspartate and serine in human myelin basic protein. Biochem Biophys Res Commun, 146, 1342-1349. , et al. (1993). Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem, 268, 3072-3083. and Clarke, S. (1982). Methylation at D-aspartyl residues in erythrocytes: possible step in the repair of aged membrane proteins. Proc Natl Acad Sci U S A, 79, 2460-2464. , Jr.

D-amino acid residues are usually discovered only after confusing experimental results are obtained. This can arise for any of the following reasons: (1) two forms of the peptide exist with identical primary structures are observed in chromatography; (2) the synthetic version of the peptide fails to elute with the native peptide in chromatography; and (3) the activity of the synthetic peptide is different from that of the native peptide. D-amino acids in peptides are commonly determined biochemically through the use of proteolytic enzymes that can discriminate between the L- and D-forms of the amino acid.

The fractions containing the desired peptides were collected into tubes using a fraction collector (FRC10 Shimadzu, Kyoto). 4. The tryptic peptides were identified by sequence analysis, and mass spectrometry. 5. The D/L ratios of the individual Asp and Asn residues in the peptides were measured by the method described in section A-2-4. Detection of the Specific D-Aspartic Acid Residues in Protein 21 A-2-4. Method for the Determination of D/L Ratio of Amino Acids in Protein or Peptides This method enables accurate analysis of amino acid enantimoers at the picomole level.

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