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. © Springer-Verlag Berlin Heidelberg 2006.
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CITATION STYLE
Fedorov, M. V., Schumm, S., & Goodman, J. M. (2006). Solvent effects and conformational stability of a tripeptide. In Lecture Notes in Computer Science (including subseries Lecture Notes in Artificial Intelligence and Lecture Notes in Bioinformatics) (Vol. 4216 LNBI, pp. 141–149). Springer Verlag. https://doi.org/10.1007/11875741_14
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