CMNS-UNDERGRAD-NEWS Archives

Daily eNews for CMNS Students

CMNS-UNDERGRAD-NEWS@LISTSERV.UMD.EDU

Options: Use Forum View

Use Monospaced Font
Show Text Part by Default
Condense Mail Headers

Message: [<< First] [< Prev] [Next >] [Last >>]
Topic: [<< First] [< Prev] [Next >] [Last >>]
Author: [<< First] [< Prev] [Next >] [Last >>]

Print Reply
Sender:
Daily eNews for CMNS Students <[log in to unmask]>
X-To:
Date:
Wed, 23 Mar 2016 07:41:43 -0400
Reply-To:
Daily eNews for CMNS Students <[log in to unmask]>
Subject:
MIME-Version:
1.0
Content-Transfer-Encoding:
8Bit
Content-Type:
text/plain; charset=UTF-8; format=flowed; delsp=yes
From:
Gene Ferrick <[log in to unmask]>
Parts/Attachments:
text/plain (40 lines)
Subject: CMNS DISTINGUISHED WOMAN FACULTY LECTURE

Description:
March 25, 2016 at 12:00 p.m.

Speaker: Patricia Babbitt, Professor, Department of Bioengineering and
Therapeutic Sciences, University of California, San Francisco

“How has nature evolved the enzymes required by living systems”

Location: Bioscience Research Building, Room 1103

Patricia Babbitt, Ph.D., University of California, San Francisco

Patricia Babbitt earned her Ph.D. in Medicinal Chemistry from the University
of California, San Francisco (UCSF). She is currently Professor of
Computational Biology in the Department of Bioengineering and Therapeutic
Sciences, the Department of Pharmaceutical Chemistry, and the California
Institute for Quantitative Biosciences (QB3). She is the Director of the UCSF
Biological and Medical Informatics Graduate Program and serves on Advisory
Boards for the UniProt Database, the Metacyc Metabolic Pathway Database, the
HHMI Scientific Review Board, and as a Deputy Editor for PLoS Computational
Biology.

Her research focuses on protein structure-function relationships in enzyme
superfamilies, aiming to understand the “architectural principles”
underlying how some protein scaffolds have evolved to enable many different
functions. To take advantage of the huge volumes of sequencing data now
available, her group uses graphical network models to summarize on a global
scale structure-function relationships in very large and functionally diverse
superfamilies. The results show that only a small proportion of these enzymes
have been functionally or structurally characterized and suggest that many
chemical capabilities remain undiscovered across the biosphere. This
observation is important for functional inference, identification of
misannotated proteins, and for providing guidance for selection of targets
for experimental and structural investigation.

Contact Person: Gene Ferrick
Contact Email: [log in to unmask]

ATOM RSS1 RSS2