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Leaving no stone unturned: Allosteric targeting of SARS-CoV-2 spike protein at putative druggable sites disrupts human angiotensin-converting enzyme interactions at the receptor binding domain

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Informatics in Medicine Unlocked 2020年 21卷 100451页

作者： Olotu, Fisayo A. Omolabi, Kehinde F. Soliman, Mahmoud E.S. Molecular Bio-computation and Drug Design Laboratory School of Health Sciences University of KwaZulu-Natal Westville Campus Durban 4001 South Africa

The systematic entry of SARS-CoV-2 into host cells, as mediated by its Spike (S) protein, is highly essential for pathogenicity in humans. Hence, targeting the viral entry mechanisms remains a major strategy for COVID-19 treatment. Although recent efforts have focused on the direct inhibition of S-protein receptor-binding domain (RBD) interactions with human angiotensin-converting enzyme 2 (hACE2), allosteric targeting remains an unexplored possibility. Therefore, in this study, for the first time, we employed an integrative meta-analytical approach to investigate the allosteric inhibitory mechanisms of SARS-CoV-2 S-protein and its association with hACE2. Findings revealed two druggable sites (Sites 1 and 2) located at the N-terminal domain (NTD) and S2 regions of the protein. Two high-affinity binders;ZINC3939013 (Fosaprepitant – Site 1) and ZINC27990463 (Lomitapide – Site 2) were discovered via site-directed high-throughput screening against a library of ~1500 FDA approved drugs. Interestingly, we observed that allosteric binding of both compounds perturbed the prefusion S-protein conformations, which in turn, resulted in unprecedented hACE2 displacement from the RBD. Estimated ΔG_binds for both compounds were highly favorable due to high-affinity interactions at the target sites. In addition, Site 1 residues;R190, H207, K206 and K187, I101, R102, I119, F192, L226, V126 and W104 were identified for their crucial involvement in the binding and stability of ZINC3939013. Likewise, energy contributions of Q957, N953, Q954, L303, Y313, Q314, L858, V952, N953, and A956 corroborated their importance to ZINC27990463 binding at the predicted Site 2. We believe these findings would pave way for the structure-based discovery of allosteric SARS-CoV-2 S-protein inhibitors for COVID-19 treatment. © 2020 The Author(s)

关键词： Allosteric targeting High-affinity binding Receptor binding domain SARS-CoV-2 Spike protein Virtual high-throughput screening

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In-Silico molecular Docking and Md Simulation Based Lead Identification of Denv-2 Inhibitor from Selected Phytochemicals of Momordica Charantia L

SSRN

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SSRN 2022年

作者： Akm, Moyeenul Huq Roney, Miah Issahaku, Abdul Rashid Soliman, Mahmoud E.S. Aluwi, Mohd Fadhlizil Fasihi Mohd Tajuddin, Saiful Nizam Faculty of Industrial Sciences and Technology Universiti Malaysia Pahang Lebuhraya Tun Razak Gambang Pahang Darul Makmur Kuantan26300 Malaysia Centre for Bio-Aromatic Research Universiti Malaysia Pahang Lebuhraya Tun Razak Gambang Pahang Darul Makmur Kuantan26300 Malaysia Department of Pharmacy School of Medicine University of Asia Pacific 74/A Green Road Dhaka1205 Bangladesh West African Centre for Computational Analysis Ghana Molecular Bio-computation and Drug Design Laboratory School of Health Sciences University of KwaZulu-Natal Westville Campus Durban4001 South Africa University of KwaZulu-Natal South Africa

Due to the annual occurrence of millions of virus diseases, dengue fever is a major global health concern. Unfortunately, there isn't a treatment that has been approved to treat dengue. Researchers are looking into DENV NS5 RdRp protease as a potential therapeutic target for discovering effective dengue treatments. In-silico methods were employed in this study to discover a DENV-2 NS5 RdRp protease inhibitor from a set of five compounds from Bitter melon (Momordica charantia L.). To obtain the hit compounds, the compounds were docked onto the active area of the DENV-2 NS5 RdRp protease. The successful compounds underwent additional testing for a study on drug-likeness similarity. Our study obtained Momordicoside-I as a lead compound which was further exposed to the Cytochrome P450 (CYP450) toxicity analysis to determine the toxicity based on docking scores and drug-likeness inquiry. The lead chemical was next subjected to a molecular dynamic (MD) simulation for 200 ns in order to confirm the stability of the docked complex and the binding posture discovered during docking tests. Overall, the lead chemical has demonstrated good medication like qualities, non-toxicity, and significant binding affinity towards RdRp enzyme. © 2022, The Authors. All rights reserved.

关键词： molecular dynamics

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Angiotensin converting enzyme inhibitors from medicinal plants: a molecular docking and dynamic simulation approach

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In silico pharmacology 2022年第1期10卷 20页

作者： Olumide Samuel Fadahunsi Olubukola Sinbad Olorunnisola Peter Ifeoluwa Adegbola Temitayo I Subair Oluwabamise Emmanuel Elegbeleye Department of Biochemistry Faculty of Basic Medical Sciences Ladoke Akintola University of Technology Ogbomoso Oyo Nigeria. Molecular Bio-Computation and Drug Design Laboratory School of Health Sciences University of KwaZulu-Natal Westville Campus Durban 4001 South Africa.

Angiotensin converting enzyme (ACE) is a key enzyme and mediator in the aetiology of high blood pressure (HBP) and hypertension. As one of the leading cause of untimely death worldwide, there is a lot of research and studies on the management and treatment of hypertension. The usage of medicinal plants in the management of hypertension as alternative to synthetic allopathic drugs is a common practice in folkloric and traditional medicine. Therefore, this study was aimed to investigate the ACE inhibitory activity of some medicinal plants which are commonly used in the treatment of HBP in southwestern part of Nigeria using extensive in-silico approach. Compounds identified in the plants through GC–MS technique, together with Lisinopril were docked against ACE protein. It was observed that only 40 of the compounds had binding affinity ≥ − 6.8 kcal/mol which was demonstrated by the standard drug (lisinopril). Interaction between the compounds and ACE was via conventional hydrogen, carbon hydrogen, alkyl, pi-alkyl, pi-carbon, and Van Der Wall bonds among others. Most of these compounds exhibited drug like properties, without violating majority of the physicochemical descriptors and Lipinski rule of 5. The ADMET evaluation revealed that only 2 compounds (cyclopentadecanone and oxacycloheptadecan-2-one) which were identified in Bacopa florinbunda plant were predicted non-toxic and thus were subjected to molecular dynamics and simulation with ACE. From the molecular dynamics and mechanics analysis, both cyclopentadecanone and oxacycloheptadecan-2-one showed high stability and inhibitory potentials when bound to ACE. Oxacycloheptadecan-2-one was more stable than lisinopril and cyclopentadecanone in the ligand–ACE complex; we therefore suggested its experimental and clinical validation as drug candidates for the treatment of hypertension.

关键词： Angiotensin converting enzyme (ACE) inhibitors Dynamics Hypertension In-silico Medicinal plants molecular docking Simulation

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Identification of differentially expressed genes present in the whole blood of Pulmonary Arterial Hypertension patients and control patients: An integrated bioinformatics approach

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Informatics in Medicine Unlocked 2020年 20卷

作者： Ezenwa, Chisom Soremekun, Opeyemi S. Nashiru, Oyekanmi Fatumo, Segun Centre for Genomics Research and Innovation National Biotechnology Agency Abuja Nigeria Molecular Bio-computation and Drug Design Laboratory School of Health Science University of KwaZulu-NatalWestville Campus Durban South Africa Uganda Medical Informatics Centre and MRC/UVRI LSHTM Uganda Research Unit Entebbe Uganda London School of Hygiene and Tropical Medicine London United Kingdom

Introduction: While Pulmonary Arterial Hypertension (PAH) remains a commonly undiagnosed disease, it remains a life-threatening disease;it is characterized by pulmonary vascular remodelling subsequently leading to heart failure. Different researches have been at the forefront of exploring drugs for treatment and molecular biomarkers for early diagnosis of PAH. Method: ology: In this study, we used an integrated bioinformatics approach to investigate Differentially Expressed Genes (DEG) in the whole blood of PAH patients relative to gender/age matching controls. Microarray dataset of the aforementioned experiment was retrieved from Gene Expression Omnibus (GEO). DEG analysis was carried out with the aid of the limma algorithm in-built in the GEO2R tool. Gene Ontology terms such as molecular function, biological process, cellular component, and pathway were investigated using the online tool Protein ANalysisTHrough Evolutionary Relationships (PANTHER). Protein-Protein interaction network was carried out using STRING. Results: From the analysis, 191 genes were down-regulated while 5 were up-regulated. Some of these genes are implicated in pathways involved in adrenaline and noradrenaline biosynthesis, angiogenesis, EGF receptor signaling pathway, and VEGF signaling pathway. Furthermore, in the ontology of molecular function, these genes are involved in transport activity, catalytic activity, and molecular transducer activity. Interestingly, the angiogenesis, adrenaline, and noradrenaline biosynthetic pathways are heavily involved in the pathogenesis and progression of PAH. Furthermore, the gene products of these predicted genes were also explored. Conclusion: The gene products (proteins) of these DEGs can be further explored as potential drug targets in the treatment of PAH. This study has also been able to establish the interaction responsible for PAH which can be explored in gene therapy. © 2020 The Authors

关键词： DEGs Enrichment analysis Integrated bioinformatics Pulmonary arterial hypertension RNAseq

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Transcription-translation error: In-silico investigation of the structural and functional impact of deleterious single nucleotide polymorphisms in GULP1 gene

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Informatics in Medicine Unlocked 2021年 22卷 100503页

作者： Soremekun, Opeyemi S. Ezenwa, Chisom Soliman, Mahmoud Chikowore, Tinashe Nashiru, Oyekanmi Fatumo, Segun Molecular Bio-computation and Drug Design Laboratory School of Health Sciences University of KwaZulu-Natal Westville Campus Durban 4001 South Africa Centre for Genomics Research and Innovation National Biotechnology Agency Abuja Nigeria MRC/Wits Developmental Pathways for Health Research Unit Department of Pediatrics Faculty of Health Sciences University of the Witwatersrand Johannesburg South Africa Sydney Brenner Institute for Molecular Bioscience Faculty of Health Sciences University of the Witwatersrand Johannesburg South Africa The African Computational Genomics (TACG) Research Group MRC/UVRI LSHTM Uganda Research Unit Entebbe Uganda Department of Non-communicable Disease Epidemiology (NCDE) London School of Hygiene and Tropical Medicine London United Kingdom

Nonsynonymous single nucleotide polymorphisms (nsSNPs) are one of the most common forms of mutations known to disrupt the product of translation thereby altering the protein structure-function relationship. GULP1 (PTB domain-containing engulfment adaptor protein 1) is an evolutionarily conserved adaptor protein that has been associated with glycated hemoglobin (HbA1c) in Genome-Wide Association Studies (GWAS). In order to understand the role of GULP1 in the etiology of diabetes, it is important to study some functional nsSNPs present within the GULP1 protein. We, therefore, used a SNPinformatics approach to retrieve, classify, and determine the stability effect of some nsSNPs. Y27C, G142D, A144T, and Y149C were jointly predicted by the pathogenic-classifying tools to be disease-causing, however, only G142D, A144T, and Y149C had their structural architecture perturbed as predicted by I-MUTANT and MuPro. Interestingly, G142D and Y149C occur at positions 142 and 149 of GULP1 which coincidentally are found within the binding site of GULP1. Protein-Protein interaction analysis also revealed that GULP1 interacted with 10 proteins such as Cell division cycle 5-like protein (CDC5L), ADP-ribosylation factor 6 (ARF6), Arf-GAP with coiled-coil (ACAP1), and Multiple epidermal growth factor-like domains protein 10 (MEGF10), etc. Taken together, rs1357922096, rs1264999716, and rs128246649 could be used as genetic biomarkers for the diagnosis of diabetes. However, being a computational study, these nsSNPs require experimental validation to explore their metabolic involvement in the pathogenesis of diseases. © 2020

关键词： GULP1 MD Simulation Nonsynonymous single nucleotide polymorphisms (nsSNPs) SNPinformatics

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Join the Fold: Video Games, Science Fiction, and the Refolding of Citizen Science

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design ISSUES 2023年第1期39卷 70-87页

作者： Milburn, Colin Buse, Katherine Dhaliwal, Ranjodh Singh Wills, Melissa Aldosari, Raida Camarador, Patrick Miller, Josh Aaron Siegel, Justin Colin Milburn is Gary Snyder Chair in Science and the Humanities and a professor of Science and Technology Studies English and Cinema and Digital Media at the University of California Davis. His research focuses on science literature and media technologies. His books include Nanovision: Engineering the Future (2008) Mondo Nano: Fun and Games in the World of Digital Matter (2015) and Respawn: Gamers Hackers and Technogenic Life (2015). Katherine Buse is an assistant professor of Media Studies at the University of Chicago. Her research focuses on digital media the environmental humanities and the cultures of science and technology. Her current book project Speculative Planetology: Science Culture and the Building of Model Worlds tells the story of how the sciences and the arts co-constructed a toolkit for thinking about planets as whole systems. Ranjodh Singh Dhaliwal is Ruth and Paul Idzik College Chair in Digital Scholarship and an assistant professor of English and Film Television and Theatre at the University of Notre Dame. His work spans media theory science and technology studies and literary criticism. His current book project Rendering: A Political Diagrammatology of Computation shows how our cultural politico-economic and epistemic formulations crystallize into hardware and software architectures. Melissa Wills is a visiting scholar in the Department of Science and Technology Studies at the University of California Davis. She completed her PhD in English at UC Davis in 2021. Her research addresses the relationship between the life sciences and science fiction. Her current book project Ruptures: Life without Germs in the Microbiome Era examines microbiology's debt to the imagination of germ-free worlds. Raida Aldosari is the lead artist on the Foldit: First Contact development team. She received her BS in Nutrition Science from the University of California Davis in 2018. She has experience as a freelance graphic designer and as a project manager for nutrition training and courses.

This article explores the value of science fiction narratives in games for citizen science. Focusing on the protein-folding game Foldit, it describes the process of modifying and redesigning the game to feature a framing narrative and other alterations to the main tutorial campaign. The campaign narrative, Foldit: First Contact, situates the practices of citizen science in an expanded context of meanings and ethical implications, promoting critical self-reflection on the relations of science and civic values. A study of player responses to Foldit: First Contact suggests the significance of science fiction and critical game design for attuning citizen scientists to the collective responsibilities of experimentation and innovation, drawing attention to the intersecting social, technical, and environmental domains in which gamers may contribute to scientific research.

关键词： citizen science science fiction video games narratives

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Genetic heterogeneity in cardiovascular disease across ancestries: Insights for mechanisms and therapeutic intervention

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Cambridge prisms. Precision medicine 2023年 1卷 e8页

作者： Opeyemi Soremekun Marie-Joe Dib Skanda Rajasundaram Segun Fatumo Dipender Gill The African Computational Genomics (TACG) Research Group Medical Research Council/Uganda Virus Research Institute and London School of Hygiene and Tropical Medicine Uganda Research Unit Entebbe Uganda. Department of Epidemiology and Biostatistics School of Public Health Imperial College London London UK. Molecular Bio-Computation and Drug Design Laboratory School of Health Sciences University of KwaZulu-Natal Westville Campus Durban South Africa. British Heart Foundation Centre of Excellence Imperial College London London UK. Centre for Evidence-Based Medicine University of Oxford Oxford UK. Faculty of Medicine Imperial College London London UK. Department of Non-Communicable Disease Epidemiology (NCDE) London School of Hygiene and Tropical Medicine London UK.

Cardiovascular diseases (CVDs) are complex in their aetiology, arising due to a combination of genetics, lifestyle and environmental factors. By nature of this complexity, different CVDs vary in their molecular mechanisms, clinical presentation and progression. Although extensive efforts are being made to develop novel therapeutics for CVDs, genetic heterogeneity is often overlooked in the development process. By considering molecular mechanisms at an individual and ancestral level, a richer understanding of the influence of environmental and lifestyle factors can be gained and more refined therapeutic interventions can be developed. It is therefore expedient to understand the molecular and clinical heterogeneity in CVDs that exists across different populations. In this review, we highlight how the mechanisms underlying CVDs vary across diverse population ancestry groups due to genetic heterogeneity. We then discuss how such genetic heterogeneity is being leveraged to inform therapeutic interventions and personalised medicine, highlighting examples across the CVD spectrum. Finally, we present an overview of how polygenic risk scores and Mendelian randomisation can foster more robust insight into disease mechanisms and therapeutic intervention in diverse populations. Fulfilment of the vision of precision medicine requires more exhaustive leveraging of the genetic variability across diverse ancestry populations to improve our understanding of disease onset, progression and response to therapeutic intervention.

关键词： ancestry cardiovascular disease genetics precision medicine therapeutics

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Structural insights into conformational stability of both wild-type and mutant Insulin Receptor Gene

Next Research

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Next Research 2024年第2期1卷

作者： Chisom Soremekun Daudi Jjingo David Kateete Oyekanmi Nash Harald Grallert Annette Peters Tinashe Chikowore Chiara Batini Opeyemi Soremekun Segun Fatumo The African Computational Genomics (TACG) Research Group MRC/UVRI and LSHTM Uganda Research Unit Entebbe Uganda Department of Immunology and Molecular Biology School of Biomedical Sciences Makerere University College of Health Sciences Kampala Uganda H3Africa Bioinformatics Network (H3ABioNet) Node Centre for Genomics Research and Innovation NABDA/FMST Abuja Nigeria Helmholtz Zentrum München German Research Center for Environmental Health (GmbH) Institute of Epidemiology Ingolstädter Landstr. 1 85764 Neuherberg Germany African Center of Excellence in Bioinformatics (ACE-B) Makerere University Kampala 10101 Uganda Department of Computer Science College of Computing and Information Sciences Makerere University P.O Box 7062 Kampala Uganda German Center for Diabetes Research (DZD) München-Neuherberg Ingolstädter Landstr. 1 85764 Neuherberg Germany Chair of Epidemiology Institute for Medical Information Processing Biometry and Epidemiology Medical Faculty Ludwig-Maximilians-Universität München Munich Germany MRC/Wits Developmental Pathways for Health Research Unit Department of Paediatrics Faculty of Health Sciences University of the Witwatersrand Johannesburg South Africa Channing Division of Network Medicine Department of Medicine Brigham and Women's Hospital and Harvard Medical School Boston MA USA Division of Genetics Department of Medicine Brigham and Women's Hospital and Harvard Medical School Boston MA USA Genetic Epidemiology Group Department of Health Sciences University of Leicester Leicester UK Leicester National Institute for Health and Care Research Biomedical Research Centre Glenfield Hospital Leicester UK Institute of Translational Genomics Helmholtz Zentrum München – German Research Center for Environmental Health Neuherberg Germany Molecular Bio-computation and Drug Design Laboratory School of Health Sciences University of KwaZulu-Natal Westville Campus Durban 4001 South Africa MRC/UVRI and LSHTM Uganda Research Unit Entebbe Uganda De

Type 2 diabetes (T2D) poses a health challenge. It can lead to complications such as heart disease, hypertension, heart failure, and stroke. Factors like obesity and lack of activity can contribute to insulin resistance. The insulin receptor gene ( INSR ) is responsible for producing insulin receptors. When this gene malfunctions, it can contribute to the development of T2D. In this study, we investigated the stability of the structure of variants of INSR using an extended molecular dynamics simulation and the perturbation effect of compound CheBI_88339 on the protein structure. During the analysis, we observed that all three systems—the wild-type INSR , the R1191Q variant, and the R1191Q variant bound to compound CheBI_88339 (R1191Q-D) reached equilibrium in 30ns without any instability. Throughout the simulation process, it was generally observed that the wild-type INSR exhibited higher stability than the R1191Q variant and R1191Q-D. The root mean square deviation (RMSD) and root mean square fluctuation (RMSF) of INSR , R1191Q and the variant bound to compound CheBI_88339 (R1191Q-D) are 9.28Å, 10.35Å, 8.65Å, 2.59Å, 2.98Å, and 2.89Å respectively. These values indicate that the mutated INSR introduced levels of deviations and flexibility in the protein structure. However, considering the variant bound to compound CheBI_88339 suggests that this drug may contribute to stabilizing the dynamics of the mutant protein. Overall, our findings shed light on the effect of genetic variants and their impact on protein stability. This research provides further insight into the dynamics of INSR and the potential of CheBI_88339 in targeting INSR . However, this study is computational, and further experimental studies are required.

关键词： Insulin receptor Type-2 diabetes molecular dynamic simulation

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26th Annual computational Neuroscience Meeting (CNS*2017) of the Organization for computational Neuroscience Antwerp, Belgium, July 15-20, 2017

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BMC NEUROSCIENCE 2017年第SUPPL 1期18卷 59-59页

作者： [Anonymous] Indiana University Purdue University Indianapolis Indianapolis IN 46032 USA Stark Neurosciences Research Institute Indiana University School of Medicine Indianapolis IN 46032 USA Department of Mathematics East Carolina University Greenville NC 27858 USA Jülich Supercomputing Centre Forschungszentrum Jülich 52425 Jülich Germany Future Systems Swiss National Supercomputing Centre 8092 Zurich Switzerland User Engagement and Support Swiss National Supercomputing Centre 6900 Lugano Switzerland Institut de Neurosciences des Systèmes Aix Marseille Univ 13005 Marseille France Simulation Lab Neuroscience Forschungszentrum Jülich Jülich Germany Department of Experimental Psychology Ghent University 9000 Ghent Belgium Donders Center for Cognitive Neuroimaging Radboud University 6525HR Nijmegen The Netherlands Department of Electrical Computer and Energy Engineering University of Colorado Boulder CO 80309 USA Department of Neurosurgery Johns Hopkins School of Medicine Baltimore MD 21287 USA Department of Neurology Johns Hopkins School of Medicine Baltimore MD 21287 USA Department of Otolaryngology Johns Hopkins School of Medicine Baltimore MD 21287 USA INSERM U968 Paris France Sorbonne Universités UPMC University Paris 06 UMR_S 968 Institut de la Vision Paris France CNRS UMR_7210 Paris France Department of Computer Architecture and Technology University of Granada (CITIC) Granada Spain Sorbonne Universités UPMC Univ Paris 06 INSERM CNRS Institut de la Vision Paris France Department of Adaptive Machine Systems Osaka University Osaka Japan Department of Computer Science University of Cergy-Pontoise Cergy-Pontoise France Department of Physics and Astronomy College of Charleston Charleston SC 29424 USA School of Physics Faculty of Science University of Sydney Sydney NSW 2006 Australia Center of Excellence for Integrative Brain Function Australian Research Council Sydney Australia Max Planck Institute for Human Cognitive and Brain Sciences Saxony Lei

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Symposia lectures

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Journal of biosciences 1999年第1期24卷 5-31页

作者： F. Parak A. Ostermann G. U. Nienhaus Nobuo Niimura William A. Eaton Stephen J. Hagen Eric R. Henry James Hofrichter Gouri Jas Lisa Lapidus Victor Muñoz Chih-chen Wang Abani Bhuyan Javant Udgaonkar Heinz Rüterians Derek N. Woolfson M. D. Finucane J. H. Lees M. J. Pandya G. Spooner M. Tuna Wilma K. Olson K. V. R. Chary E. Westhof I. G. Wool C. C. Correll V. I. Ivanov S. A. Bondarenko E. M. Zdobnov A. D. Beniaminov E. E. Minyat N. B. Ulyanov Dale B. Wigley Nobuo Shimamoto Takashi Kinebuchi Hiroyuki Kabata Osamu Kurosawa Masao Washizu Barbara Baird David Holowka H. Belrhali P. Nollert A. Royant J. P. Rosenbusch E. M. Landau E. Pebav-Peyroula Anil K. Lala Patrick R. D’Silva Daniela Pietrobon Paolo Pinton Paulo Magalhaes Anna Chiesa Marisa Brini Tullio Pozzan Rosario Rizzuto M. Montai Shu-Rong Wang José L. Carrascosa B. Bhattacharyya Ian A. Wilson Dinakar M. Salunke Kurt Drickamer Anne Imberty A. Surolia Louise N. Johnson Michal Neeman S. M. Prince K. McLuskey R. J. Cogdell K. McAuley N. W. Isaacs G. Venturoli F. Drepper J. C. Williams J. P. Allen X. Lin P. Mathis R. van Grondelle Wolfgang Junge T. Tsukihara K. Shinzawa-Itoh R. Nakashima E. Yamashita M. J. Fei N. Inoue T. Tomizaki C. Peters Libeu S. Yoshikawa Patrick Chaussepied Keiichi Namba Marie-France Carlier Fariza Ressacl Valerie Laurent Thomas Loisel Coumaran Egile Philippe Sansonetti Dominique Pantaloni Manju Bansal E. W. Knapp M. G. Ullmann A. Amadei B. L. de Groot M. A. Ceruso M. Paci H. J. C. Berendsen A. Di Nola V. Di Francesco P. J. Munson J. Garnier Sung-Hou Kim Jean-Michel Claverie Ian C. P. Smith P. T. Callaghan Bruce Cornell Ratna S. Phadke Kazuhiko Kinosita D. Goldfarb I. Qromov C. Shutter I. Pecht P. Manikandan R. Carmieli T. Shane David S. Moss Clare E. Sansom Jeremy K. Cockcroft Ian J. Tickle Huub C. P. Driessen J. Raul Grigera Ramen K. Poddar Charles R. Cantor Barry Robson Jean Garnier John Helliwell Sunney I. Chan Ronald Rock Physik-Department El7 Technische Universität München Garching Abteilung Biophysik Universität Ulm Ulm Advanced Science Research Center Japan Atomic Energy Research Institute Japan Laboratory of Chemical Physics NIDDK National Institutes of Health Bethesda USA National Lab of Biomacromolecules Institute of Biophysics Beijing China National Centre for Biological Sciences Bangalore Institute of Biophysical Chemistry University of Frankfurt Frankfurt/Main Germany Centre for Biomolecular Design and Drug Development University of Sussex UK Rutgers University Piscataway USA Department of Chemical Sciences Tata Institute of Fundamental Research Mumbai India IBMC-CNRS Strasbourg France Department of Biochemistry and Molecular Biology The University of Chicago Chicago USA Engelhardt Institute of Molecular Biology RAS Moscow Russia Sir William Dunn School of Pathology University of Oxford Oxford UK Structural Biology Center National Institute of Genetics Japan Faculty of Engineering Kyoto University Kyoto Advance Co. Tokyo Japan Department of Chemistry and Chemical Biology Cornell University Ithaca Institute de Biologie Structurale Joseph Fourier Grenoble Cedex 1 France Biomembrane Lab Department of Chemistry and Biotechnology CenterIndian Institute of Technology Bombay Powai Mumbai India Dept of Biomedical Sciences Univ. of Padova Italy Dept. Exp. Diagn. Med. Sect. Gen. Pathol Ferrara Italy Department of Biology University of California San Diego La Jolla USA Chinese Academy of Sciences Institute of Biophysics Beijing China Centra Nacional de Biotecnología CSIC. Campus de la Universidad Autónoma de Madrid Cantoblanco Spain Dept.of Biochemistry Bose Institute Calcutta-54 India The Scripps Research Institute La Jolla National Institute of Immunology New Delhi India Glycobiology Institute Department of Biochemistry University of Oxford Oxford UK Centre de Recherches sur les Macromolécules Végétales-CNRS Grenoble cedex 9 France Molecular Biophysics Uni

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