BackgroundThe prediction of ligand binding or protein structure requires very accurate force field potentials – even small errors in force field potentials can make a 'wrong' structure (from the billions possible) more stable than the single, 'correct' one. However, despite huge efforts to optimize them, currently-used all-atom force fields are still not able, in a vast majority...
AffiliationsInstitute of Protein Research, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, RussiaAlexei V Finkelstein AuthorsSearch for Alexei V Finkelstein in:PubMed • Google Scholar Corresponding ... author Correspondence to Alexei V Finkelstein. Authors’ original submitted files for images Below are the links to the authors’ original submitted files for images. Authors’ original file for
Funnel-like landscapes are widely used to visualize protein folding. It might seem that any funnel-like energy landscape helps to avoid the `Levinthal paradox', i.e. to avoid sampling the impossibly large number of conformations for a folding protein. This cunning suggestion, reinforced by beautiful drawings of the energy funnels, stimulated some simple models of protein folding...
We present a general approach to the prediction of 3-D folds of protein chains from their amino acid sequences. The approach is based on the use of the self-consistent molecular field theory for long-range interactions, the use of 1-D statistical mechanics for short-range interactions and on the discovery that there is and should only be a relatively small discrete set of folding...
