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From protein folding to protein function and biomolecular binding by energy landscape theory
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Center for Theoretical Biological Physics, University of California San Diego, San Diego, USA.
2010 (English)In: Current opinion in pharmacology (Print), ISSN 1471-4892, E-ISSN 1471-4973, Vol. 10, no 6, 709-714 p.Article in journal (Refereed) Published
Abstract [en]

Protein folding and function are inherently linked sharing a joined funneled energy landscape. In this theoretical framework, the integration of simulations, structural information, and sequence data has led to quantitatively explore, understand, and predict biomolecular binding and recognition, key processes in pharmacology, as a natural extension of the selective self-binding found in protein folding. Computer simulations based on these principles have made valuable contributions to understanding protein and RNA folding, protein-protein interactions, and protein-metabolite/RNA-metabolite interactions.

Place, publisher, year, edition, pages
Elsevier Ltd , 2010. Vol. 10, no 6, 709-714 p.
National Category
Pharmacology and Toxicology
Identifiers
URN: urn:nbn:se:umu:diva-37290DOI: 10.1016/j.coph.2010.09.012ISI: 000284749400016PubMedID: 20951644OAI: oai:DiVA.org:umu-37290DiVA: diva2:358874
Available from: 2010-10-25 Created: 2010-10-25 Last updated: 2017-12-12Bibliographically approved

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