The first Café Scientifiques were held in Leeds, in the UK, in 1998. From there, café’s gradually spread across the globe. Café Scientifique is a place where anyone can come to explore the latest ideas in science and technology. Meetings are a forum for debating science issues and promoting public interest in science. The goal of the Café’s is simply to have regularly scheduled sessions for informal discussions of scientific topics. Meetings start with a short talk from the speaker, who is usually a scientist or a writer on science, to introduce the topic followed by an hour or so of questions and answers and general discussion.
Information on upcoming meetings can be found at: http://www.chemistry.msu.edu/sciencecafe/
Lansing Community College also conducts science cafés. For more information see: http://www.lcc.edu/science/cafe_scientifique.aspx
Chemistry Teachers Monthly Meeting
When: 2nd Monday
of each month during the academic year
Time: 7:00 pm
Location: 481W Chemistry Building, Michigan State University
Information about past meetings and upcoming meeting topics can be found at our Chemistry Teachers Homepage. Anyone interested is welcome to attend the meetings. If you know of any teachers who might enjoy being a part of this group, please pass on the information to them. Questions? Contact Gavin Reid (email@example.com) or Kathy Severin (firstname.lastname@example.org).
Contact Kathy Severin if you'd like to be added to our teacher e-mail list.
Local Section Meeting - Wednesday, January 12, 2011
Shifting Shapes - How to See a Protein's Moves
The Max T. Rogers Distinguished Lectureship will be held on Wednesday, January 12, 2011 at 4:10 pm in room 138 Chemistry Building on the MSU campus. Professor Ann McDermott, the Esther Breslow Professor of Biological Chemistry at Columbia University will present a lecture "Shifting Shapes - How to See a Protein's Moves". Local section members are invited to attend the lecture and the wine and cheese reception in her honor which follows.
To carry out their remarkable cellular functions, proteins must have shapes that are malleable, and undergo a wide variety of conformational exchange processes on different timescales. Nuclear Magnetic Resonance offers an integrated tool to study a protein's structures, their populations, and the rates of interconversion among them. The importance of flexibility and the possibilities to study it with NMR and other biophysical methods will be illustrated using the example of our studies of Triose Phosphate Isomerase, a glycolytic enzyme. The NMR and other biophysical data on this enzyme highlight several key concepts in enzymology such as preorganization and compression, and also raise interesting issues regarding the coordination of the conformational exchange process to the progress of chemical reaction.