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Dr. Englander's laboratory is interested in macromolecular structure, dynamics, and function and has developed the use of hydrogen exchange (HX) approaches in protein and nucleic acid studies. Many hydrogens in proteins and nucleic acids are in continual exchange with the hydrogens in solvent water. These can provide literally hundreds of probe points that are sensitive to structure, structure change, internal dynamics, energy, and functional interactions at identifiable positions throughout a macromolecule. Work in this lab has explained the chemistry of protein and nucleic acid HX processes and has formulated the physical models that appear to explain the ways in which internal motions in proteins and nucleic acids determine the HX rates of their individual protons. The lab has developed and is using special hydrogen exchange methods that can measure the specific parts of any protein involved in any function, the protein folding process as it occurs on a sub-second time scale, the energetic stability of individual bonding interactions, structure change, etc. Methods in use include the range of protein biophysical techniques including 2D NMR and mutational analysis. The lab has in recent years produced a coherent explanation for how proteins fold. Present work is directed at testing and enlarging this model.
Selected Publications: Krishna, M.M.G., S.W. Englander (2006) A unified mechanism for protein folding. Predetermined pathways and optional errors. J. Mol. Biol., in press. Englander, S.W. (2006) Hydrogen exchange and mass spectrometry: a historical perspective. J. Amer. Soc. Mass. Spec., in press. Krishna, M.M.G., H. Maity, J.N. Rumbley, Y. Lin, and S.W. Englander (2006) Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism. J. Mol. Biol. 359:1410-1419. Maity, H., J.N. Rumbley, S.W. Englander (2006) Functional role of a protein foldon: An W-loop foldon controls the alkaline transition in cytochrome c. Proteins 63:349-355. |
