Publications with Fulltext

Permanent URI for this collectionhttps://hdl.handle.net/20.500.14288/6

Browse

Filters

2017 - 20182

Advanced Search

Filter by

Settings

Quartile: search.filters.quartile.N/ASubject: search.filters.subject.Biophysics

Search Results

Now showing 1 - 2 of 2
  • Thumbnail Image
    PublicationOpen Access
    PRISM-EM: template interface-based modelling of multi-protein complexes guided by cryo-electron microscopy density maps (corrigendum)
    (International Union of Crystallography, 2018) Nussinov, Ruth; Department of Chemical and Biological Engineering; Kuzu, Güray; Keskin, Özlem; Gürsoy, Attila; Faculty Member; Department of Chemical and Biological Engineering; College of Engineering; Graduate School of Sciences and Engineering; N/A; 26605; 8745
    A revised Table 6 and Supporting Information are provided for the article by Kuzu et al. [(2016 ), Acta Cryst. D72, 1137-1148].
  • Thumbnail Image
    PublicationOpen Access
    Causality, transfer entropy, and allosteric communication landscapes in proteins with harmonic interactions
    (Wiley, 2017) Department of Chemical and Biological Engineering; Hacısüleyman, Aysima; Erman, Burak; Faculty Member; Department of Chemical and Biological Engineering; College of Engineering; N/A; 179997
    A fast and approximate method of generating allosteric communication landscapes in proteins is presented by using Schreiber's entropy transfer concept in combination with the Gaussian Network Model of proteins. Predictions of the model and the allosteric communication landscapes generated show that information transfer in proteins does not necessarily take place along a single path, but an ensemble of pathways is possible. The model emphasizes that knowledge of entropy only is not sufficient for determining allosteric communication and additional information based on time delayed correlations should be introduced, which leads to the presence of causality in proteins. The model provides a simple tool for mapping entropy sink-source relations into pairs of residues. By this approach, residues that should be manipulated to control protein activity may be determined. This should be of great importance for allosteric drug design and for understanding the effects of mutations on function. The model is applied to determine allosteric communication in three proteins, Ubiquitin, Pyruvate Kinase, and the PDZ domain. Predictions are in agreement with molecular dynamics simulations and experimental evidence.