Protein dynamics and allostery: An NMR view

Shiou Ru Tzeng, Charalampos G. Kalodimos

Research output: Contribution to journalReview articlepeer-review

182 Scopus citations


Allostery, the process by which distant sites within a protein system are energetically coupled, is an efficient and ubiquitous mechanism for activity regulation. A purely mechanical view of allostery invoking only structural changes has developed over the decades as the classical view of the phenomenon. However, a fast growing list of examples illustrate the intimate link between internal motions over a wide range of time scales and function in protein-ligand interactions. Proteins respond to perturbations by redistributing their motions and they use fluctuating conformational states for binding and conformational entropy as a carrier of allosteric energy to modulate association with ligands. In several cases allosteric interactions proceed with minimal or no structural changes. We discuss emerging paradigms for the central role of protein dynamics in allostery.

Original languageEnglish (US)
Pages (from-to)62-67
Number of pages6
JournalCurrent Opinion in Structural Biology
Issue number1
StatePublished - Feb 2011

Bibliographical note

Funding Information:
This work was supported by the National Science Foundation (MCB-0618259).


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