Chemical Biology

Special Seminar: Erol Akçay, Princeton

Mon, 2013-02-04 10:00
Speaker: 
Dr. Erol Akçay
Princeton University

New frontiers in social evolution theory

Host: Josh Plotkin (Biology)
Location: 

Lynch Lecture Hall

 

Cooperation between organisms is a major driving force of biological organization at all levels, from single cells to whole ecosystems. Understanding the evolutionary dynamics of cooperation and other social traits therefore is a central goal of evolutionary theory. I will talk about my recent work that aims to advance the frontiers of social evolution theory in two directions.

 

Special Seminar: Emilia Huerta-Sanchez, University of California, Berkeley

Mon, 2013-01-28 10:00
Speaker: 

Dr. Emilia Huerta-Sanchez

University of California, Berkeley

 

Detecting and characterizing natural selection from next generation sequencing data

 

Host: Charles Epstein (Math)

Location: 

Lynch Lecture Hall

 

Special Seminar: Sharon Aviran, University of California, Berkeley

Thu, 2013-01-24 10:00
Speaker: 

Dr. Sharon Aviran

University of California, Berkeley

 

High-throughput RNA structure analysis from chemical footprinting experiments

 

Host: Randy Kamien (Physics)

Location: 

Lynch Lecture Hall

 

New regulatory roles continue to emerge for both natural and engineered RNAs, many of which have specific structures essential to their function. This highlights a growing need to develop technologies that enable rapid and accurate characterization of structural features within complex RNA populations. Yet, available techniques that are reliable are also vastly limited by technological constraints, while the accuracy of popular computational methods is generally poor. These limitations thus pose a major barrier to comprehensive determination of structure from sequence.

Special Seminar: Kirill Korolev, MIT

Tue, 2013-01-22 10:00
Speaker: 

Dr. Kirill Korolev

Massachusetts Institute of Chemistry

 

The interplay between ecology and evolution in cancerous tumors and expanding populations

 

Host: Andrea Liu

Location: 

Lynch Lecture Hall

 

Special Seminar: Eleni Katifori, MPI-Goettingen

Thu, 2013-01-17 10:00
Speaker: 

Dr. Eleni Katifori

Max Planck Institute - Goettingen

 

The evolution of leaf vasculature: deciphering the design of optimal loopy architectures

 

Host: Douglas Jerolmack (Earth and Environmental Sciences)

Location: 

Lynch Lecture Hall

 

Hirschmann Visiting Professor Lecture 1 - James Skinner, Univ. Wisconsin

Tue, 2013-02-19 16:00
Speaker: 

James L. Skinner, University of Wisconsin, Madison

 


Lecture 1

The mystery of water and its phases
Tuesday, February 19, 2013
4:00 PM
Reception to follow in Nobel Hall

Location: 

Carolyn Lynch Lecture Hall

Chemical Biophysics Mini-Symposium

Thu, 2013-01-10 12:30 - 17:30
Speaker: 

 

Speakers include: 

 

Steven Artandi

Stanford University

 

Lorena Beese

Duke University

 

Robert Weinberg

Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology

 

Cynthia Wolberger

Howard Hughes Medical Institute, The Johns Hopkins University

Location: 

 

Lynch Lecture Hall, Chemistry Building

 

Topic: The Chemical Biology of Cancer

 

Click here for more details.

 

Elizabeth Rhoades, Yale; Special Biophysical Seminar

Fri, 2012-12-07 13:00
Speaker: 

Elizabeth Rhoades, Yale University

 

Where the Crystal Structure Ends:  Defining 'Structure' in Disordered Proteins

Location: 

Lynch Lecture Hall

Donald Voet

Photo: 
First Name: 
Donald
Last Name: 
Voet
Official Title: 
Emeritus Associate Professor of Chemistry

Biological Chemistry

Contact Information
Office Location: 
349 N
Email: 
voet@sas.upenn.edu
Phone: 
(215) 898-6457
Education: 
  • B.S. California Institute of Technology (1960)
  • Ph.D. Harvard University (1967)
  • Post Doc at MIT, Cambridge, MA, 1966–1969 in the laboratory of Alexander Rich
  • Member ACS and AAAS
  • Visiting Scholar, Weizmann Institute of Science, Rehovot, Israel, 1993 and 1998
  • Editor-in-Chief, Biochemical and Molecular Biology Education.
Research Interests: 

We are studying the structures of biologically interesting molecules by X-ray crystallography in an effort to understand their structure-function relationships. Current projects include:

 

Yeast inorganic pyrophosphatase

Pyrophosphatases are essential enzymes that catalyze the hydrolysis of inorganic pyrophosphate to phosphate and, in doing so, drive the many biosynthetic reactions that yield pyrophosphate (e.g., polypeptide and polynucleotide synthesis) to completion. We have determined the refined 2.7-angstrom resolution structure of yeast inorganic pyrophosphatase, a dimeric enzyme of identical 286-residue subunits. We are presently determining the X-ray structures of selected mutant forms of this enzyme, both alone and in complex with inhibitors of this enzyme. The results of these studies, when correlated with the enzymological characteristics of the mutant enzymes, should lead to the formulation of a catalytic mechanism of inorganic pyrophosphatases as well as a greater understanding of biological phosphoryl transfer reactions in general.

 

Granulocyte -macrophage colony-stimulating factor (GM-CSF)

GM-CSF is a protein growth factor (cytokine) that stimulate the differentiation, proliferation, and activation of white blood cells known as granulocytes and macrophages. The therapeutic use of GM-CSF therefore holds considerable promise for the treatment of immunosuppressive conditions such as AIDS and the consequences of cancer chemotherapy. Indeed, GM-CSF is presently in clinical use to facilitate bone marrow transplantation. We have determined the refined X-ray structure of human GM-CSF to 3.0-angstrom resolution. We plan to determine the X-ray structures of selected mutant varieties of human GM-CSF in an effort to understand how GM-CSF interacts with its cell surface receptor. We also intend to determine the X-ray structure of the human GM-CSF receptor, both alone and in complex with GM-CSF. 

 

 

The x-ray structure of yeast inorganic pyrophosphatase. A 286-residue monomer unit of this homodimeric enzyme is shown with its polypeptide backbone represented in ribbon form embedded in its solvent accessible surface. The side chains of its active site residues are shown in ball-and-stick form.

Selected Publications: 

Voet , Voet; Biochemistry, 3rd Edition Student Companion Site

Department of Chemistry

231 S. 34 Street, Philadelphia, PA 19104-6323

215.898.8317 voice | 215.573.2112 fax | web@chem.upenn.edu

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