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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology.ORCID iD: 0000-0002-1685-4735
KTH, Centres, Science for Life Laboratory, SciLifeLab. KTH, School of Biotechnology (BIO), Proteomics and Nanobiotechnology.ORCID iD: 0000-0002-4066-2776
2016 (English)In: Journal of Visualized Experiments, ISSN 1940-087X, E-ISSN 1940-087X, no 107, e53168Article in journal (Refereed) PublishedText
Abstract [en]

Enzyme catalysis evolved in an aqueous environment. The influence of solvent dynamics on catalysis is, however, currently poorly understood and usually neglected. The study of water dynamics in enzymes and the associated thermodynamical consequences is highly complex and has involved computer simulations, nuclear magnetic resonance (NMR) experiments, and calorimetry. Water tunnels that connect the active site with the surrounding solvent are key to solvent displacement and dynamics. The protocol herein allows for the engineering of these motifs for water transport, which affects specificity, activity and thermodynamics. By providing a biophysical framework founded on theory and experiments, the method presented herein can be used by researchers without previous expertise in computer modeling or biophysical chemistry. The method will advance our understanding of enzyme catalysis on the molecular level by measuring the enthalpic and entropic changes associated with catalysis by enzyme variants with obstructed water tunnels. The protocol can be used for the study of membrane-bound enzymes and other complex systems. This will enhance our understanding of the importance of solvent reorganization in catalysis as well as provide new catalytic strategies in protein design and engineering.

Place, publisher, year, edition, pages
Journal of Visualized Experiments , 2016. no 107, e53168
Keyword [en]
Chemistry, Issue 107, Enzyme catalysis, thermodynamics, water, dynamics, membrane protein, kinetics, transition state theory, protein engineering, hydrophobic effect
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:kth:diva-182168DOI: 10.3791/53168ISI: 000368577400007ScopusID: 2-s2.0-84954533987OAI: oai:DiVA.org:kth-182168DiVA: diva2:904091
Funder
Swedish Research Council, 621-2013-5138Science for Life Laboratory - a national resource center for high-throughput molecular bioscience
Note

QC 20160218

Available from: 2016-02-18 Created: 2016-02-16 Last updated: 2016-02-18Bibliographically approved

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Kurten, CharlotteSyren, Per-Olof
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