The Rowland Institute at Harvard

Biophysical Chem Lab


Jeff Hoch
Alan Stern


Human Prolactin

NMR Data Processing

Structure Calculations

Group Alumni

Peter Connolly
Claudio Chuaqui
Eric LaRosa
Kuo-Bin Li
George Maalouf
John Osterhout

Rowland Home

Laboratory of Biophysical Chemistry

Our laboratory works on problems related to the physical basis for the biological activity of proteins. Broadly, this includes their structure, dynamics, stability, and interactions with other molecules. Some specific questions we are interested in include
  • The relationship of the dynamics of a binding loop, in a protein that acts as a neurotoxin by binding to the acetylcholine receptor, to its biological activity.
  • The role played by various forces in determining the stability, and conformational changes, of the hormone Prolactin.
  • The nature of protein-water interactions, especially their contribution to protein stability.

We employ a variety of physical and computational methods, including nuclear magnetic resonance, circular dichroism, fluoresence, and ultraviolet/visible absorption spectroscopies, measurements of water activity, modern spectrum analysis, and molecular dynamics simulations.

LSIII, a neurotoxin
Human Prolactin
NMR Data Processing
Macromolecular structure calculations

Copyright © 2002 The Rowland Institute at Harvard.

Last modified Thursday, October 09, 2003.