Item Details

title

Investigating the Role of Conformational Flexibility in tRNA Aminoacylation

author

Banerjee, Papri

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.

contributor

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

type

Dissertation