J Adamcik, R Mezzenga - Angewandte Chemie International …, 2018 - Wiley Online Library
Protein folding involves a large number of steps and conformations in which the folding protein samples different thermodynamic states characterized by local minima. Kinetically …
Conspectus Are all protein interactions fully optimized? Do suboptimal interactions compromise specificity? What is the functional impact of frustration? Why does evolution not …
S Piana, JL Klepeis, DE Shaw - Current opinion in structural biology, 2014 - Elsevier
Highlights•The accuracy of physical models used in protein-folding simulations is assessed.•This assessment is based on data from very long molecular dynamics …
Y Shen, Y Wang, IW Hamley, W Qi, R Su… - Progress in Polymer …, 2021 - Elsevier
Chirality is one of the most important structural features in biological systems. Peptides, as a class of small biomolecules, can self-assemble into various chiral supramolecular polymers …
The traditional view that proteins possess absolute functional specificity and a single, fixed structure conflicts with their marked ability to adapt and evolve new functions and structures …
Genomes 5 has been completely revised and updated. It is a thoroughly modern textbook about genomes and how they are investigated. As with previous Genomes editions …
J Kubelka, J Hofrichter, WA Eaton - Current opinion in structural biology, 2004 - Elsevier
How fast can a protein possibly fold? This question has stimulated experimentalists to seek fast folding proteins and to engineer them to fold even faster. Proteins folding at or near the …
Equilibrium molecular dynamics simulations, in which proteins spontaneously and repeatedly fold and unfold, have recently been used to help elucidate the mechanistic …
M Fuxreiter, I Simon, P Friedrich, P Tompa - Journal of molecular biology, 2004 - Elsevier
Intrinsically unstructured proteins (IUPs) are devoid of extensive structural order but often display signs of local and limited residual structure. To explain their effective functioning, we …