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Theoretical studies of peptidic structures. Environmental effects (1993)

Fraga, Serafin ; Thornton, Stephen E.

Springer

Theoretical chemistry accounts 85 (1993), S. 61-67

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ISSN: 1432-2234

Keywords: Theoretical simulation ; Peptide ; Tertiary structure ; pH solvation ; H-bond ; Salt-bridge

Source: Springer Online Journal Archives 1860-2000

Topics: Chemistry and Pharmacology

Notes: Summary The peptide Asp-Glu-Arg-Ser has been studied using the software package maPSI, with simulation of the pH conditions and the influence of the solvent. It is concluded, in agreement with the experimental observation, that in solution DERS is distorted from a true β-turn conformation, without H-bond but stabilized by a weak salt-bridge between the side chains of the Glu and Arg residues.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01374577

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