BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Memento EPFL//
BEGIN:VEVENT
SUMMARY:Electric Fields and Enzyme Catalysis
DTSTART:20180320T161500
DTEND:20180320T173000
DTSTAMP:20260407T020334Z
UID:8955fcd705ef0288e9a3226d83e12b5f81ea105ab7b894312476e3f9
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Steven Boxer\, Department of Chemistry \, Stanford Unive
 rsity \nSteven Boxer is the Camille Dreyfus Professor in the Department o
 f Chemistry at Stanford University.  His research interests are in biophy
 sics: the interface of physical chemistry\, biology and engineering.  Top
 ics of current interest include: electrostatics and dynamics in proteins\,
  especially related to enzyme catalysis\; excited state dynamics of green 
 fluorescent protein\, especially split GFP\, with applications in biotechn
 ology\; electron and energy transfer mechanisms in photosynthesis\; and th
 e fabrication of artificial systems to simulate\, manipulate and image bio
 logical membranes.  He has served on the scientific advisory board of man
 y start-ups in the general area of biotechnology\, and as an advisor to go
 vernment and non-profit organizations in the U.S. and around the world.  
 He is the recipient of several awards and is an elected Fellow of the Amer
 ican Academy of Arts and Sciences\, the Biophysical Society and the Nation
 al Academy of Sciences. \n\nDuring his talk\, Prof. Boxer will present t
 he vibrational Stark effect his lab has developped to probe electrostati
 cs in proteins where they can report on functionally important electric fi
 elds.  In a model enzyme\, the field sensed at the bond involved in enzym
 atic catalysis is correlated with the activation energy of the reaction it
  catalyzes\, including variations in a series of mutants and variants usin
 g non-canonical amino acids. This provides the first direct connection bet
 ween electric fields and function and can be used to re-interpret results 
 already in the literature and provide a framework for parsing the electros
 tatic contribution to catalysis. \n 
LOCATION:SV 1717 https://plan.epfl.ch/?room==SV%201717
STATUS:CONFIRMED
END:VEVENT
END:VCALENDAR
