Disclaimer: The following information is drawn from materials prepared by candidates for promotion to full professor. It is intended to illustrate activities and materials that might support promotion. In using these materials, please note the following: *The Provost (and, in some cases, the President) are the University officers authorized to approve promotions. All levels of review below these officers are advisory. *Only Departments are empowered to propose promotions, and the Divisional Dean is charged with transmitting such proposals to the Provost or returning them to the Department. *The judgment of the Department, Dean, and Provost will therefore be critical to assessing qualification for promotion. *Materials considered by the Department, Dean, and Provost will also (and always) include confidential evaluations obtained from outside the University. Materials considered by the Provost will include the confidential evaluations of the Dean and Department, and those considered by the Dean will include the confidential evaluations of the Department. *Thus, the following materials are ONLY PART of a complete proposal for promotion, whereas promotion is based on the ENTIRE proposal. Therefore, it should not be assumed that a record comparable to that below will necessarily result in promotion, or that a record not comparable to that below will fail to result in promotion. The Departmental Chair is likely to be the best source of advice as to whether promotion is feasible and, when it is not, what additional activity may result in qualification for promotion. *This document has been prepared as a tool for use by associate professors in the Division of the Biological Sciences. Other individuals who may find it informative are Department Chairmen, Section Heads, Committee Chairmen, senior faculty and potential recruits. Its intent is to help guide individuals and their departments as they think about promotion to Professor. This document is not intended to list the elements that every promotion proposal will be expected to address. The following information is presented for information purposes only and is not intended to create any contract or agreement, and its contents are subject to addition, deletion, and change without prior notice.
Name:		Tobin R. Sosnick, Ph.D.

Department of Primary Appointment:

Biochemistry and Molecular Biology

Secondary appointments:

Institute for Biophysical Dynamics

Present rank:

Associate Professor

Present track:

Research Scholar Track

Proposed rank:

PROFESSOR

Proposed track:

RESEARCH SCHOLAR (TENURE)

DEPARTMENT: What is the candidate's field or specialization?

Folding of protein and RNA molecules using experiment and computation.

LAY SUMMARY:

Tobin Sosnick is a scholar in two important and related yet independent fields of molecular biology. Namely, he is elucidating how protein and RNA molecules go from their nascent state to their functional form. Each of these molecules is a string-like polymer that folds up into a functional structure. The information for folding is inherent in the sequence of the amino acids in proteins, but there are countless pathways that these molecules must negotiate on the way to condensing into their unique functional form. Tobin Sosnick has developed and applied approaches to track the important steps in these folding pathways, using both experimental and computational approaches. Furthermore, the insights he has generated go beyond the description of the precise folding paths of selected macromolecules; rather, they shed light on how protein and RNA molecules function after maturation; for example, how they associate and interact with one another.

Tobin Sosnick has served the educational mission of our Division by providing teaching in relevant graduate courses, advising undergraduates in the biophysical area, chairing graduate student recruitment for BMB and its teaching cluster, being co-PI on an NIH training grant and winning a HHMI training grant for a new graduate program that he also chairs.

Mr. Sosnick has provided administrative service by serving on and chairing several committees in BMB, the IBD, the Mol. Biosciences graduate student cluster, the BSD Research Advisory Committee, the BSD NMR facility, and the University’s Committee on Core Facilities.

PRESENTATIONS

(since November 1996)

March 10, 2007 9^th Hopkins Folding Meeting, Maryland

December 11, 2006 University of Montreal, Dept. of Biochemistry. Montreal, Canada

December 8, 2006 3^rd Annual Symposium on Computational and Theoretical Biology, Rice University

September 24, 2006 Gordon Research Conference on Computational Aspects of Biomolecular NMR “Statistical coil model of the unfolded state: Resolving the reconciliation problem”, Aussois, France

July 14, 2006 MRSEC “Bag Lunch” Series “Making Ugly Proteins Beautiful: A Cinderella Story.” Univ. of Chicago

May 3, 2006 Midwest Protein Folding Conference, “The consensus folding transition state of acyl phosphatase discerned using ψ-analysis” Notre Dame, IN

March 24, 2006 The DePaul Colloquium Series in Bioinformatics and Biological Computing, “Integrating multiple length scales in protein folding”

March 20, 2006 Penn State University, Dept. of Chemistry, “Principles and structural characterization of protein and RNA folding pathways.” State College, PA

February 13, 2006 Gordon Research Conference on Isotopes in Biological & Chemical Science, “Amide isotope effects in protein folding: How much are H-bonds worth? When do they form?” Ventura, CA

February 13, 2006 Univ. of Calif, San Francisco, “Transition states discerned using ψ-analysis” Miniature Protein Folding Festival, Prof. K. Dill host

February 6, 2006 Northwestern University, Biophysics Series, “Protein folding: Experimental characterization of transition state(s) with simulations of unfolded and native states.” Chicago, IL

January 8, 2006 Gordon Research Conference, Protein Dynamics, Ventura, CA Session Chair

December 16, 2005 Center for Computational Biology & Bioinformatics, Indiana University School of Medicine, “Protein folding: Structure of transition and denatured states; Integrating multiple length-scales in folding simulations”, Indianapolis, IN

December 5, 2005 Amgen, Thousand Oaks, Calif. “Structural identity of protein folding transition states discerned using ψ-analysis”

October 3, 2005 First European Conference on Chemistry for Life Sciences, Rimini, Italy. Invited speaker. “Structural identity of protein folding transition states discerned using ψ-analysis”

September 28, 2005 Computations in Science seminar series, University of Chicago, “Integrating multiple length scales in protein folding”

May 31, 2005 American Crystallographic Society Annual Mtg, Florida, invited speaker to session on “Chain Collapse and Hydrogen Bond Formation in Protein Folding”

April 15, 2005 Northern Illinois University, Center for Biochemical and Biophysical Studies, “The folding of complex RNA structures, ribozymes”

March 17, 2005 University of Washington, Department of Biochemistry, “Protein folding pathways discerned using ψ-analysis and other methods” Seattle, WA

March 10, 2005 Harvard University Woodward Lecture Series in the Chemical Sciences/Physical Chemistry Seminar, “Protein folding pathways discerned using ψ-analysis and other methods”, Boston, MA

January 25, 2005 University of Wisconsin, Dept. of Chemistry seminar, “Protein folding pathways discerned using ψ-analysis and other methods”, Madison, WI

November 12, 2004 University of Missouri, “Multiple pathways in protein folding investigated using ψ-analysis, and the relationship between RNA folding rates and topology” Department of Biochemistry seminar

August 14, 2004 “RNA-The Other Biomolecule” Session Chair, Protein Society Annual Meeting

July 21, 2004 University of Tokyo, “Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis along with tests of the Diffusion-Collision Model”, Tokyo, Japan

July 16, 2004 Osaka University, “Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis along with tests of the Diffusion-Collision Model”, Osaka, Japan

July 15, 2004 Kobe University, “Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis along with tests of the Diffusion-Collision Model”, Kobe, Japan

July 14, 2004 International Symposium on “Structure and Dynamics in Macromolecular Systems with Specific Interaction” OUMS'04, Osaka, Japan. Invited speaker, “Chain collapse and hydrogen bond formation in protein folding.”

June 3, 2004 RNA Society Annual Meeting, platform talk, “Reduced Contact Order and RNA folding rates.”

March 2004 NSLS-II workshop, Brookhaven National Laboratory. “SAXS and collapse in protein folding.”

January 20, 2004 Gordon Research Conference, Metals in Biology, “Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis.” Ventura, CA

January 12, 2004 Gordon Research Conference, Protein Dynamics, “Discerning the structure and energy of multiple transition states in protein folding using ψ-analysis.” Ventura, CA

December 2003 National Tsing Hua University, Taiwan, “Theoretical Approaches to Self Assembly in Protein and RNA Folding.” 4 lectures.

March 2003 Washington University “Barriers, Hydrogen bond formation and pathway heterogeneity in protein folding. Dept. of Biochemistry and Molecular Biophysics.

May 2002 Annual RNA Society Meeting, “The intrinsic rate-limiting step in tertiary RNA folding”. Platform session, Madison, Wisconsin

May 2002 American Crystallography Association, Annual Meeting, San Antonio, TX, “Thermodynamic origin of the stability of a thermophilic ribozyme.”

May 2002 Stanford Linear Accelerator “Limiting steps, Hydrogen bond formation and pathway heterogeneity in protein folding”

April 2002 Stanford University, “Tertiary RNA folding: Kinetics and the origins of thermophilic stability.”

April 2002 University of Illinois, Urbana, “Kinetics of Hydrogen bond formation in protein folding.” Theoretical Biophysics Seminar, Beckman Institute,

March 2002 Johns Hopkins University, Department of Biophysics and Biophysical Chemistry “Rate limiting steps in RNA and protein folding”

March 2002 University of Pennsylvania, Department of Biochemistry and Biophysics “Hydrogen bond formation and pathway heterogeneity in protein folding.”

March 2002 New York University, Department of Chemistry “Hydrogen bond formation and pathway heterogeneity in protein folding.”

March 2002 Columbia University, Department of Biochemistry and Mol. Biophysics “Rate limiting steps in RNA and protein folding”

February 2002 University of California, Santa Barbara, Dept. of Chemistry and Biochemistry “Rate limiting steps in RNA and protein folding”

February 2002 The Scripps Research Institute “Rate limiting steps in RNA and protein folding”

February 2002 University of Illinois, Chicago, Dept. of Chemistry, “H-bond formation, multiple pathways, and ultra-fast events in protein folding.”

February 2002 Illinois Institute of Technology “How do Proteins fold to the Native Structures?”

January 2002 Conference “Self Organizing Biomolecules - The Evolving Picture”, Sante Fe “Rate limiting steps in RNA folding”

November 2001 Indiana University, Biochemistry Seminar Series “Tertiary RNA folding: Kinetics and the origins of thermophilic stability”,

July 2001 Telluride Workshop on Landscapes and Protein Folding. “H-bond formation and Pathway heterogeneity”

June 2001 Biological Sciences Division, Argonne National Lab “Ultra-fast events, multiple pathways, and kinetic isotope in protein folding”.

March 2001 The 6th Annual Johns Hopkins Folding Meeting. “Secondary structure formation, kinetic isotope effects and pathway heterogeneity in protein folding. “ (session chair)

November 2000 International Symposium on Advances in Bioinorganic Chemistry, Tata Institute of Fundamental Research, Bombay, India, “Metal ions and the thermodynamics and kinetics of tertiary RNA folding.”

May 2000 Annual RNA Society Meeting, “Small-angle X-ray scattering studies of ribozyme folding”. Platform session, Madison, WI.

September 2000 New York University, Dept. of Chemistry “Protein and RNA folding”

April 2000 Argonne National Lab, Basic Energy Sciences Synchrotron Radiation Center Second Users’ Meeting, “Small-angle X-ray scattering studies of RNA and ribozyme folding at the APS.”

March 2000 Purdue University, Structural Biology Seminar Series “Large ribozyme folding, thermodynamics, kinetics and co-transcriptional folding,

February 2000 Annual Biophysical Society, “Thermodynamics and the fast, error-free folding of a large ribozyme”, Platform session, New Orleans, LA

June 1999 Telluride Workshop on Rugged Landscapes,. “RNA and protein folding”

May 1998 Annual RNA Society Meeting, “Rapid RNA folding under kinetic control Intermediates & kinetic traps in RNA folding revealed by CD, catalytic act. & circular permutation.” Madison, WI.

May 1998 The Argonne National Lab/University of Chicago Cross-disciplinary Symposium, “Function Follows Form: How Biological Molecules Adopt Their Shapes.”

November 1997 The University of Chicago, Department of Chemistry “Misfolding, nucleation and the role of secondary structure in protein folding.”

July 1997 Telluride Workshop on Rugged Landscapes.

November 1996 Harvard University, Dept. of Chemistry and Chemical Biology, “The role of helix formation in the folding of fully helical coiled coil.”