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| Presented by Institut Teknologi Bandung and University of Groningen |
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Proteins are macromolecules which have vital functions in all biological processes. Proteins function as biocatalysts, transporters, providing mechanical support and immune protection, generating movement, transmitting nerve impulses, as well as controlling growth and differentiation. Properties of protein are largely dictated by its three dimensional structure which is determined by its amino acid sequence. In addition, many proteins are posttranslationally modified which includes glycosylation, acetylation, hydroxylation, carboxylation, phosphorylation, chemical rearrangement of side chains, and peptide-bond cleavage. These modifications and cleavages are essential features of protein formation and function. Protein is the most versatile molecule in which its structure could be modified by a subtle change in amino acid and/or in the environment and hence could alter its function. Modification of protein from its original structure, especially in human, may lead to severe diseases. Hemoglobin is a fascinating red blood cell protein which efficiently carries oxygen from the lungs to the tissues, and to transport carbon dioxide and hydrogen ions back to the lungs. A single amino acid residue substitution, namely glutamate into valine (E6V), decreases the solubility of deoxyhemoglobin, resulting in fibrous aggregates which then block small capillaries and impair blood flow. This blood disease is called as sickle-cell anemia. Such desease was originally believed tobe conveyed by either viruses or bacteria infections. In the last few decades, neurological diseases were found to be transmitted by proteins which are termed prions. These diseases include bovine spongiform encephalopathy (commonly referred to as mad cow disease), Creutzfeldt-Jakob disease in human beings, and crappie in sheep. The leading scientist who proposed the misfolding protein transmitted diseases, Stanley Prusiner, was awarded the Nobel Prize in physiology or medicine in 1997. Why amino acid substitutions affect proteins function, which in some cases lead to severe diseases as described above? Nowadays, this question can be explained at molecular level by investigating the change of protein folding. Since 1957, Christian Anfinsen has highlighted that a primary structure of a protein contains information about its folding pathway. Amino acid substitutions, therefore, to a certain extent, will affect information about the folding pathway of proteins and may give rise to the change of their tertiary structures. Thus, understanding of protein folding mechanisms is a vital for anticipating or handling any diseases related to misfolding of proteins. Protein folding problems, however, still become the challenging field of study for many scientists to date. Scientists from various fields have worked intensively to understand the mystery of protein folding. The recent advanced in experimental techniques and instrumentations as well as theories have gradually unraveled the mystery. Growing numbers of publications related to the proteins folding is the evident for the fast progress of the field. The GSL 2008 will focus on the recent progress in the protein folding research and their related implications of its misfolding, which in many cases may cause severe human diseases. The Lecture will consist of one day seminar and two days workshop. The seminar will present distinguish scientists from The Netherlands, Germany, United Kingdom, Japan, and Indonesia. Research results from other Indonesian researchers will also be presented either oral or in the form of posters. Awards will be given to three best posters. Scopes : 1.Protein folding problem: protein folding pathways, misfolding and human diseases, molecular chaperonin, and protein disulfide isomerase. 2.Folding dynamics and catalysis: protein transports, molecular dynamics simulations, enzymes, and protein engineering (including site-directed mutagenesis). 3.Protein and DNA analysis: Proteomics, protein-drugs interaction, protein bioinformatics, QSAR, biosensors, analytical biochemistry, real-time PCR and DNA mutations. Objectives Seminar in GSL 2008 is aimed to facilitate Indonesian scientist to communicate and discuss their research results with distinguish international researchers, as well as to publish their research result to the community. This event surely will widen and enriched our knowledge in the field of protein folding and dynamics. Introduction to several new techniques in this field, as well as hands-on practical experience to new comers will accelerate the understanding of protein folding and its implications. Advisory board Prof. Emmy Suparka, Institut Teknologi Bandung Akhmaloka, , PhD., Institut Teknologi Bandung Achmad Saifuddin Noer, PhD., Institut Teknologi Bandung Prof. Jaap J. Beintema, University of Groningen Prof. Arnold J. M. Driessen, University of Groningen Prof. Bauke W. Dijkstra, University of Groningen for detail you can download GSL2008 leaflet below   |
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