Tertiary structure prediction of C-peptide of ribonuclease A by multicanonical algorithm

dc.creatorHansmann, Ulrich H. E.
dc.creatorOkamoto, Yuko
dc.date1998-06-12
dc.date.accessioned2026-07-07T05:56:12Z
dc.date.available2026-07-07T05:56:12Z
dc.descriptionWe have performed multicanonical Monte Carlo simulations of C-peptide of ribonuclease A. It is known by CD and NMR experiments that this peptide has high alpha-helix content in aqueous solution and that the side-chain charges of residues Glu-2$^-$ and His-12$^+$ play an important role in the stability of the alpha-helix. In order to confirm these experimental implications, we have used two analogues of the peptide with charged and neutral side chains of Glu-2 and His-12. Two dielectric functions, distance-dependent and constant, are considered to study the effects of solvent contributions. All the simulations were started from random initial conformations. Various thermodynamic quantities such as average helicity as a function of residue number and average distance between two side chains as a function of temperature are calculated. The results are found to be in accord with the implications of CD and NMR experiments. The lowest-energy conformation obtained has an alpha-helix from Ala-4 to Gln-11 in complete agreement with the corresponding structure deduced from an X-ray crystallography experiment of ribonuclease A. It is shown that the salt bridge between the side chains of Glu-2$^-$ and Arg-10$^+$, which is known to exist from both NMR and X-ray experiments, is formed only when the side chains are properly charged. Its formation is greatly enhanced when the distance-dependent dielectric function is used.
dc.descriptionLatex, 3 Figures
dc.identifierhttps://arxiv.org/abs/physics/9806017
dc.identifierhttp://arxiv.org/abs/physics/9806017
dc.identifierJ. Phys. Chem. B 102 (1998) 653-656
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/87520
dc.subjectChemical Physics
dc.subjectBiological Physics
dc.subjectQuantitative Biology
dc.titleTertiary structure prediction of C-peptide of ribonuclease A by multicanonical algorithm
dc.typetext

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