1H-nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH

✍ Scribed by Arno Bundi; Kurt Wüthrich

• Book ID: 102762887
• Publisher: Wiley (John Wiley & Sons)
• Year: 1979
• Tongue: English
• Weight: 615 KB
• Volume: 18
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1979.360180206

✦ Synopsis

The 'H-nmr chemical shifts and the spin-spin coupling constants of the common amino acid residues were measured in solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH in D2O and H20, and the influence of X on the nmr parameters of the neighboring residues Gly 2 and Ala 4 was investigated. The titration parameters for the side chains of Asp, Glu, Lys, Tyr, and His were determined. The pK, values obtained in D20, with the use of pHmeter readings with a combination glass electrode uncorrected for istope effects, were 0.06 pH units higher in the acidic range and 0.10 pH units higher in the basic range than the corresponding pK, values in HzO. This suggests that the present data are suitable "random-coil" 'H-nmr parameters for conformational studies of polypeptide chains in D2O and H20 solutions.