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Site-Specific Incorporation of Chemical Probes into Proteins for NMR

A Quamrul Hassan*

Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

ACS Chem. Biol., 2008, 3 (9), pp 524–526

DOI: 10.1021/cb800215d

Publication Date (Web): September 19, 2008

* Corresponding author, aqhassan@mit.edu.

Abstract

The ability to incorporate chemical probes into peptides is of great importance because it can render novel functionality to proteins and greatly expand our capacity to investigate complex biological systems. A methodology developed by the Schultz laboratory provides a unique strategy to incorporate chemical probes as unnatural amino acids into proteins by “expanding the genetic code” of the host cell. A recent application of this methodology that allows the site-specific incorporation of three NMR-active probes into proteins demonstrates the potential for researchers to explore avenues that are not easily achievable with existing methods.

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Published In Issue September 19, 2008
Article ASAPSeptember 19, 2008
Received: September 4, 2008

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Points of View

Site-Specific Incorporation of Chemical Probes into Proteins for NMR

Abstract

Tools

SciFinder Links

History

Recommend & Share

Related Content

In vivo Incorporation of Unnatural Amino Acids to Probe Structure, Dynamics, and Ligand Binding in a Large Protein by Nuclear Magnetic Resonance Spectroscopy

Design and Applications of Bifunctional Small Molecules: Why Two Heads Are Better Than One

A Novel Class of Small Molecule Inhibitors of Hsp90

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