Year: 2013
Type: dissertation
Abstract: Using bioinformatic tools to model the conformational and thermodynamic properties of proteins we address the hypothesis launched by Susan Lindquist et al. in 2012 in the work ""Quantitative Analysis of HSP90-Client Interactions Reveal Principles of Substrate Recognition", suggesting that the destabilization of the kinase domain in a subset of protein kinases makes them substrates of HSP90 protein in a reaction mediated by de CDC37 cochaperone.--¿Do thermodynamic parameters determine HSP90-cient binding within the kinase superfamily?-- Results -Stability prediction of minimized structures
Authors: Pujols Pujol, Jordi, Universitat Autònoma de Barcelona. Facultat de Biociències
Language: English
Topic: Heat shock proteins research
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W7029030223