Solvent effects and conformational stability of a tripeptide

Maxim V. Fedorov, Stephan Schumm, Jonathan M. Goodman

Research output: Chapter in Book/Report/Conference proceedingConference contribution book

4 Citations (Scopus)

Abstract

In this work we are trying to gain an insight on the molecular mechanisms of the salt effects on conformational stability of proteins with use of fully atomistic Molecular Dynamics simulations techniques. Such 'in silico' approach allows us to obtain quite realistic data on the time and scale resolutions that are unavailable for both 'in vitro' and 'in vivo' experimental techniques. We investigated a trialanine peptide which is the one of the simplest examples of biomolecules, bearing the essential features of proteins.

Original languageEnglish
Title of host publicationComputational life sciences II
EditorsMR Berthold, R Glen, I Fischer
Place of PublicationBerlin
Pages141-149
Number of pages9
DOIs
Publication statusPublished - 2006

Publication series

NameLecture Notes in Computer Science
PublisherSpringer
Volume4216

Keywords

  • 2-dimensional vibrational spectroscopy
  • molecular-dynamics
  • Trialanine
  • water
  • transition
  • simulation
  • mechanism
  • proteins

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