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Prof. Harold A. Scheraga
Todd Professor of Chemistry Emeritus,
Baker Laboratory of Chemistry and Chemical Biology,
Cornell University - U.S.A.
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Prof. Harold A. Scheraga, the author of “Protein Structure” and “Theory of Helix-coil Transition” and up to 1100 articles in scientific journals, is a world-renowned giant with many results unanimously regarded as major milestones in the history of protein folding. His consistent endeavors in the past 60 years bring us not only considerable scientific accomplishments but also sincere appreciation and deep gratitude.
In recognition of Prof. Harold A. Scheraga's outstanding achievements in life science, we hold this celebration. We believe you agree with us that this precious occasion would gain much deeper connotations, by fostering the sincere hope that more experts would devote their life and intelligence to human health, rather than just honor Prof. Harold A. Scheraga. Also, what makes us more proud of this great event is that it would bring global experts and professionals together to contribute their scientific efforts in making human progress.
| Prof. Scheraga has made over the years numerous seminal contributions to the field of physical chemistry of biomacromolecules. He recognized early-on the importance of advanced computational methods for conformational and structural analysis of proteins, and was one of the pioneers in the development and application of sophisticated empirical force-field based simulation techniques, which have had a long-lasting impact on biomolecular science. Scheraga has also been a key player behind the theory of the helix-coil transition in polypeptides, and performed important experimental work to study helical propensities of amino acids. He also contributed significantly to the experimental understanding of protein folding and the role of disulphide bond formation in the process. Prof. Scheraga's seminal contributions over 60 years of scientific work have led to a very broad recognition, including numerous prizes and a long-time membership in the National Academy of Sciences of the USA. |
---From Gilad Haran,Weizmann Institute of Science, Israel |
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Protein Folding and Diseases |
Proteins take center stage in directing the working of living cells. Every conceivable role within human bodies is played by proteins, from catalysis chemical reactions to defence against alien attack.
The process of protein folding is remarkably efficient, but sometimes it can go wrong. This can have harmful consequences, as the incorrect folding of proteins is thought to be the cause of diseases, including Alzheimer's disease, Parkinson's disease, one of the inherited forms of emphysema, new variant CJD, Cystic Fibrosis, Type 2 Diabetes, and even some cancers are all related to the abnormal folding of proteins within the body.
This forum brought together an international experts to discuss current thinking on protein folding and misfolding research, mechanisms, Molecular Chaperones, drug discovery and therapeutic strategies for treating protein folding diseases. |
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Sponsors |
Call for Sponsors!
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| Please join us in this grant event and we sincerely hope that, by holding this kind of celebration, worldwide experts and professionals in protein and peptide areas would work together to make more contributions to life sciences. |
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Tentative Program
Ceremony & Academic Symposium for One Great Scientist's Golden Life
Chairs: Dr. Istvan Simon, Hungarian Academy of Sciences, Hungary
Dr. Mahesh Narayan, Asst. Prof. of Chemistry, University of Texas at El Paso, USA
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Data |
Time |
Activities |
April 22, 2008
18:30-19:10
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Tuesday
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18:30-19:10
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Keynote Speech
Title: Determination of Protein Structure and Protein Folding Pathways with a Physics-Based Coarse-Grained Force Field
Prof. Harold A. Scheraga, Todd Professor of Chemistry Emeritus, Baker
Laboratory of Chemistry and Chemical Biology, Cornell University - USA |
April 23, 2008
9:00-12:00
(Wednesday) |
9:00-9:20 |
Opening Session and Celebration Activities CHAIR: Mahesh Narayan |
9:20-12:00 |
Session 1: Exploring Protein Folding and Misfolding Pathways
| 9:20-9:50 |
Title: The Ecdysone Receptor - A Protein Capable of Adopting A Finite Number of Alternative Robust Functional Conformations
Dr. Ronald J. Hill, Chief Research Scientist, CSIRO Molecular and Health Technologies, Australia |
| 9:50-10:20 |
Title: Folding Pathways of Disulfide-Containing Proteins
Dr. Salvador Ventura Zamora, Associate Professor in Biochemistry and Molecular Biology. Universitat Autonoma de Barcelona, Spain |
| 10:20-10:50 |
Title: The Development of in situ photo-CIDNP NMR Techniques for Protein Folding Studies and the Characterization of Structurally Ill-Defined States
Dr. K. Hun Mok, Lecturer, University of Dublin, Ireland |
| 10:50-11:00 |
Tea Break |
| 11:00-11:30 |
Title: Bioinformatic Approaches to Studying Protein Folding
Dr. Ashley M. Buckle, NHMRC Senior Research Fellow, Monash University, Australia |
| 11:30-12:00 |
Title: Exploring Protein Folding and Misfolding Pathways
Dr. Krishna M. G. Mallela,University of Colorado Health Sciences Center, USA |
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| April 23, 2008
13:30-16:50
(Wednesday) |
13:30-14:30 |
Session 2: Protein Misfolding and Disease
| 13:30-14:00 |
Title: TPPP/p25: from Unfolded Protein to Neurological Disorder
Dr. Judit Ovádi, Professor, Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Hungary |
| 14:00-14:30 |
Title: Amyloid-like Neuronal Tau Induces Neuron Apoptosis
Dr. Rongqiao He, Professor, Institute of Biophysics, Chinese Academy of Sciences, China |
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14:30-15:30 |
Session 3: Molecular Chaperones and Cell Signalling
| 14:30-15:00 |
Title: Enhancing Refolding Yields of Proteins using Small Molecule Chemical Chaperones
Dr. Rajiv Bhat, Professor, School of Biotechnology, Jawaharlal Nehru University, India |
| 15:00-15:30 |
Title: Hierarchy of vibrational Patterns in Proteins seems to image their biological Functions
Dr. Bent Havsteen, Professor emeritus, University of Kiel, Denmark |
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| 15:30-15:40
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Tea Break
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15:40-17:40 |
Session 4: Protein Folding and Drug Design
| 15:40-16:10 |
Title: Protein-Protein Interactions that Determine Immunogenicity: Design of "de-immunized" Factor VIIII Proteins as Potential Therapeutics for Hemophilia A
Dr. Kathleen P. Pratt, Assistant Member, Puget Sound Blood Center, USA |
| 16:10-16:40 |
Title: Phenylketonuria–a Model for a Treatable Genetic Protein Misfolding Disease with Loss of Function
Dr. Ania Muntau, Project Leader, Dr. von Hauner Children's Hospital, Germany |
| 16:40-17:10 |
Title: Dissecting the Role of the Oxidoreductase, Protein Disulfide Isomerase, during the Maturation of ER-Processed Proteins
Dr. Mahesh Narayan, Assistant Professor, Department of Chemistry at University of Texas–El Paso, USA |
| 17:10-17:40 |
Title: Construction of an Effective Free Energy Landscape from Single-Molecule Time Series
Dr. Tamiki Komatsuzaki, Professor, Research Institute for Electronic Science, Hokkaido University, Japan |
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Contact Us:
Ms. Melody Lin,
Program Coordinator
Email: melody@bitlifesciences.com
Add: 26 Gaoneng Street, Room 405,
Dalian High-tech Zone,
Dalian, LN 116025, China
Tel: 0086-411-84799609 ext. 810
Fax: 0086-411-84799629 |
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