Computational approaches to understand the atomistic drivers of enzyme catalysis

Enzymes readily perform chemical reactions several orders of magnitude faster than their uncatalyzed versions in ambient conditions with high specificity, making them attractive design targets for industrial purposes. Traditionally, enzyme reactivity has been contextualized through transition-state theory (TST), in which catalytic strategies are described by their ability to minimize the activation energy to cross the reaction barrier through a combination of ground-state destabilization (GSD) and transition-state stabilization (TSS). While excellent progress has been made to rationally design enzymes, the complexity of the design space and the highly optimized nature of enzymes make general application of these approaches difficult. This thesis presents a set of computational methods and applications in order to investigate the larger perspective of enzyme-assisted kinetic processes.

Name thesis:degree_name

Doctoral

Department dc:contributor.department

Massachusetts Institute of Technology. Department of Chemical Engineering

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2021

Author dc:creator

• Seelam, Natasha.

Advisor dc:contributor.advisor

• Bruce Tidor.

• Chemical Engineering.

Statement dc:rights

• MIT theses may be protected by copyright. Please reuse MIT thesis content according to the MIT Libraries Permissions Policy, which is available through the URL provided.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

https://hdl.handle.net/1721.1/130672

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/130672