Notice of Online Archive

  • This page is no longer being updated and remains online for informational and historical purposes only. The information is accurate as of the last page update.

    For questions about page contents, contact the Communications Division.

Roger Rowlett, professor and chair of chemistry at Colgate University, will give two campus talks Monday as part of the Consortium for Research Opportunities in the Plant Sciences (CROPS), a new program in which Lafayette serves as lead institution with funding from the National Science Foundation and the Camille and Henry Dreyfus Foundation.

Rowlett will speak on “From Spots to Molecules: A Protein X-ray Crystallography Primer” in the Biochemistry Survey class taught by David Husic, John D. and Frances H. Larkin Professor and head of chemistry, at 11 a.m. in Hugel Science Center room 205. He will present a seminar on “Is Nature Stuck in a Rut? Convergent Evolution in the Carbonic Anhydrases as Revealed by Site-Directed Mutagenesis of the b-Enzyme” at noon in room 205.

Cosponsored by the chemistry department, both CROPS talks are open to campus. Pizza will be served prior to the second talk.

“The first talkwill provide an introduction as to how structural biochemists utilize the technique known as x-ray crystallography to determine the detailed three-dimensional structure of a complex protein molecule,” says Husic. “Such information provides insight into the structural and functional relationships in proteins. The second talk will discuss how this methodology, as well as other biochemical and molecular techniques, have been applied to study the details of the reaction mechanism and regulation of the enzyme carbonic anhydrase from the widely studied mustard plant, Arabidopsis thaliana.”

Rowlett’s research interests include enzymology, the isolation, purification, and characterization of enzymes, especially experimental kinetics; protein engineering, the specific alteration of enzyme structure using recombinant DNA methods; and X-ray crystallography, the determination of three-dimensional protein structures from X-ray diffraction by single protein crystals.

Categorized in: News and Features