Home WakeSpace Scholarship › Electronic Theses and Dissertations

Investigating the Role of Conformational Flexibility in tRNA Aminoacylation

Electronic Theses and Dissertations

Item Files

Item Details

abstract
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.
subject
contributor
Banerjee, Papri (author)
Alexander, Rebecca W (committee chair)
Cho, Samuel (committee member)
Bierbach, Ulrich (committee member)
Colyer, Christa (committee member)
Dos Santos, Patricia (committee member)
date
2012-06-12T08:35:42Z (accessioned)
2014-06-12T08:30:07Z (available)
2012 (issued)
degree
Chemistry (discipline)
embargo
2014-06-12 (terms)
identifier
http://hdl.handle.net/10339/37251 (uri)
language
en (iso)
publisher
Wake Forest University
title
Investigating the Role of Conformational Flexibility in tRNA Aminoacylation
type
Dissertation

Usage Statistics