Investigating the Role of Conformational Flexibility in tRNA Aminoacylation

Proteins are dynamic macromolecules. According to Koshland's classical "induced fit" model of enzyme regulation, proteins have essential conformational flexibility for ligand binding, which promotes catalysis by structural rearrangement. Proteins undergo structural rearrangements to bind ligands, regulate access to a catalytic site, or release products. The energetic contribution of protein flexibility to catalysis is not well understood, despite numerous high resolution crystal structures available for numerous proteins bound with their corresponding ligands.

Grantor dc:publisher

Wake Forest University

Year dc:date.issued

2012

Author dc:creator

• Banerjee, Papri

Language dc:language.iso

en

Handle dc:identifier.uri

http://hdl.handle.net/10339/37251

OAI identifier oai:identifier

oai:wakespace.lib.wfu.edu:10339/37251