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Publisher Correction: Protein-altering variants associated with body mass index implicate pathways that control energy intake and expenditure in obesity

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Nature genetics 2018年第5期50卷 766-767页

作者： Valérie Turcot Yingchang Lu Heather M Highland Claudia Schurmann Anne E Justice Rebecca S Fine Jonathan P Bradfield Tõnu Esko Ayush Giri Mariaelisa Graff Xiuqing Guo Audrey E Hendricks Tugce Karaderi Adelheid Lempradl Adam E Locke Anubha Mahajan Eirini Marouli Suthesh Sivapalaratnam Kristin L Young Tamuno Alfred Mary F Feitosa Nicholas G D Masca Alisa K Manning Carolina Medina-Gomez Poorva Mudgal Maggie C Y Ng Alex P Reiner Sailaja Vedantam Sara M Willems Thomas W Winkler Gonçalo Abecasis Katja K Aben Dewan S Alam Sameer E Alharthi Matthew Allison Philippe Amouyel Folkert W Asselbergs Paul L Auer Beverley Balkau Lia E Bang Inês Barroso Lisa Bastarache Marianne Benn Sven Bergmann Lawrence F Bielak Matthias Blüher Michael Boehnke Heiner Boeing Eric Boerwinkle Carsten A Böger Jette Bork-Jensen Michiel L Bots Erwin P Bottinger Donald W Bowden Ivan Brandslund Gerome Breen Murray H Brilliant Linda Broer Marco Brumat Amber A Burt Adam S Butterworth Peter T Campbell Stefania Cappellani David J Carey Eulalia Catamo Mark J Caulfield John C Chambers Daniel I Chasman Yii-Der I Chen Rajiv Chowdhury Cramer Christensen Audrey Y Chu Massimiliano Cocca Francis S Collins James P Cook Janie Corley Jordi Corominas Galbany Amanda J Cox David S Crosslin Gabriel Cuellar-Partida Angela D'Eustacchio John Danesh Gail Davies Paul I W Bakker Mark C H Groot Renée Mutsert Ian J Deary George Dedoussis Ellen W Demerath Martin Heijer Anneke I Hollander Hester M Ruijter Joe G Dennis Josh C Denny Emanuele Di Angelantonio Fotios Drenos Mengmeng Du Marie-Pierre Dubé Alison M Dunning Douglas F Easton Todd L Edwards David Ellinghaus Patrick T Ellinor Paul Elliott Evangelos Evangelou Aliki-Eleni Farmaki I Sadaf Farooqi Jessica D Faul Sascha Fauser Shuang Feng Ele Ferrannini Jean Ferrieres Jose C Florez Ian Ford Myriam Fornage Oscar H Franco Andre Franke Paul W Franks Nele Friedrich Ruth Frikke-Schmidt Tessel E Galesloot Wei Gan Ilaria Gandin Paolo Gasparini Jane Gibson Vilmantas Giedraitis Anette P Gjesing Penny Gordon-Larsen Mathias Gorski Hans-Jörgen Montreal Heart Institute Université de Montréal Montreal Quebec Canada. Division of Epidemiology Department of Medicine Vanderbilt-Ingram Cancer Center Vanderbilt Epidemiology Center Vanderbilt University School of Medicine Nashville TN USA. Charles Bronfman Institute for Personalized Medicine Icahn School of Medicine at Mount Sinai New York NY USA. Genetics of Obesity and Related Metabolic Traits Program Icahn School of Medicine at Mount Sinai New York NY USA. Department of Epidemiology University of North Carolina Chapel Hill NC USA. Human Genetics Center University of Texas School of Public Health University of Texas MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences University of Texas Health Science Center at Houston Houston TX USA. Broad Institute of MIT and Harvard Cambridge MA USA. Department of Genetics Harvard Medical School Boston MA USA. Division of Endocrinology and Center for Basic and Translational Obesity Research Boston Children's Hospital Boston MA USA. Center for Applied Genomics Division of Human Genetics Children's Hospital of Philadelphia Philadelphia PA USA. Quantinuum Research LLC San Diego CA USA. Estonian Genome Center University of Tartu Tartu Estonia. Division of Epidemiology Department of Medicine Institute for Medicine and Public Health Vanderbilt Genetics Institute Vanderbilt University Nashville TN USA. Institute for Translational Genomics and Population Sciences LABioMed at Harbor-UCLA Medical Center Torrance CA USA. Wellcome Trust Sanger Institute Hinxton UK. Department of Mathematical and Statistical Sciences University of Colorado Denver CO USA. Wellcome Trust Centre for Human Genetics University of Oxford Oxford UK. Department of Biological Sciences Faculty of Arts and Sciences Eastern Mediterranean University Famagusta Cyprus. Max Planck Institute of Immunobiology and Epigenetics Freiburg Germany. Department of Biostatistics and Center for Statistical Genetics University of M

In the version of this article originally published, one of the two authors with the name Wei Zhao was omitted from the author list and the affiliations for both authors were assigned to the single Wei Zhao in the author list. In addition, the ORCID for Wei Zhao (Department of Biostatistics and Epidemiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA) was incorrectly assigned to author Wei Zhou. The errors have been corrected in the HTML and PDF versions of the article.

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computational approaches to understanding protein aggregation in neurodegeneration

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Journal of molecular Cell biology 2014年第2期8卷 104-115页

作者： Rachel L. Redler David Shirvanyants Onur Dagliyan Feng Ding Doo Nam Kim Pradeep Kota Elizabeth A. Proctor Srinivas Ramachandran Arpit Tandon Nikolay V. Dokholyan Department of Biochemistry and Biophysics University of North Carolina at Chapel Hill Chapel Hill NC USA Program in Cellular and Molecular Biophysics University of North Carolina at Chapel Hill Chapel Hill NC USA Curriculum in Bioinformatics and Computational Biology University of North Carolina at Chapel Hill Chapel Hill NC USA Center for Computational and Systems Biology University of NorthCarolina at Chapel Hill chapel Hill NC USA Department of Physics and Astronomy Ctemson University Ctemson SC USA Cellular Growth Mechanisms Section Laboratory of Cell and Developmental Signaling Frederick National Laboratory for Cancer Research Frederick MD USA Division of Basic Sciences Fred Hutchison Cancer Research Center Seatt{e WA USA

The generation of toxic non-native protein conformers has emerged as a unifying thread among disorders such as Alzheimer＇s disease, Parkinson＇s disease, and amyotrophic lateral sclerosis. Atomic-level detail regarding dynamical changes that facilitate protein aggre- gation, as well as the structural features of large-scale ordered aggregates and soluble non-native oligomers, would contribute signifi- cantly to current understanding of these complex phenomena and offer potential strategies for inhibiting formation of cytotoxic species. However, experimental limitations often preclude the acquisition of high-resolution structural and mechanistic information for aggregating systems. computational methods, particularly those combine both aU-atom and coarse-grained simulations to cover a wide range of time and length scales, have thus emerged as crucial tools for investigating protein aggregation. Here we review the current state of computational methodology for the study of protein self-assembly, with a focus on the application of these methods toward understanding of protein aggregates in human neurodegenerative disorders.

关键词： protein aggregation molecular dynamics protein folding neurodegeneration

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In‐Membrane Chemical Modification (IMCM) for Site‐Specific Chromophore Labeling of GPCRs

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Angewandte Chemie 2015年第50期127卷

作者： Lukas Sušac Casey O'Connor Raymond C. Stevens Kurt Wüthrich Department of Integrative Structural and Computational Biology The Scripps Research Institute 10550 North Torrey Pines Road La Jolla CA 92037 (USA) Departments of Biological Sciences and Chemistry Bridge Institute University of Southern California 3430 South Vermont Avenue Los Angeles CA 90089 (USA) Skaggs Institute of Chemical Biology The Scripps Research Institute 10550 North Torrey Pines Road La Jolla CA 92037 (USA) Institute of Molecular Biology and Biophysics ETH Zurich Otto‐Stern‐Weg 5 8093 Zurich (Switzerland)

We present in‐membrane chemical modification (IMCM) for obtaining selective chromophore labeling of intracellular surface cysteines in G‐protein‐coupled receptors (GPCRs) with minimal mutagenesis. This method takes advantage of the natural protection of most cysteines by the membrane environment. Practical use of IMCM is illustrated with the site‐specific introduction of chromophores for NMR and fluorescence spectroscopy in the human κ‐opioid receptor (KOR) and the human A 2A adenosine receptor (A 2A AR). IMCM is applicable to a wide range of in vitro studies of GPCRs, including single‐molecule spectroscopy, and is a promising platform for in‐cell spectroscopy experiments.

关键词： Fluoreszenzspektroskopie G‐Protein‐gekoppelte Rezeptoren Membranproteine NMR‐Spektroskopie Positionsspezifische Markierung

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Cover Picture: The Exploding Genetic Code (ChemBioChem 12/2014)

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ChemBioChem 2014年第12期15卷 1689-1689页

作者： Dr. Edward A. Lemke European Molecular Biology Laboratory Structural and Computational Biology Unit Cell Biology and Biophysics Unit Meyerhofstrasse 1 69117 Heidelberg (Germany)

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11th German Conference on Chemoinformatics (GCC 2015) Abstracts

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JOURNAL OF CHEMINFORMATICS 2016年第SUPPL 1期8卷 1-27页

作者： [Anonymous] GDCh-CIC Division Associated Board Member Beilstein-Institut zur Förderung der Chemischen Wissenschaften Trakehner Str. 7-9 60487 Frankfurt Germany. ufechner@beilstein-institut.de. Division Medicinal Chemistry Amsterdam Institute for Molecules Medicines and Systems (AIMMS) VU University Amsterdam The Netherlands. Centre for Bioinformatics Uni Hamburg Bundesstr. 43 20146 Hamburg Germany. Sanofi-Aventis Deutschland GmbH 65926 Frankfurt am Main Germany. stefan.guessregen@***. Sanofi-Aventis Deutschland GmbH 65926 Frankfurt am Main Germany. GlaxoSmithKline Stevenage SG1 2NY UK. nicola.j.richmond@***. Discngine Paris 75011 France. Organisch-Chemisches Institut Westfälische Wilhelms-Universität Münster Germany. marwin.segler@wwu.de. Organisch-Chemisches Institut Westfälische Wilhelms-Universität Münster Germany. Bundeskriminalamt Wiesbaden Central Analytics II 65173 Wiesbaden Germany. Department of Chemistry and Biochemistry University of California Santa Barbara CA 93111 USA. shea@chem.ucsb.edu. Department of Chemistry and Biochemistry University of California Santa Barbara CA 93111 USA. Chemistry Department Ludwig-Maximilians-Universität München Butenandtstr. 7 81377 Munich Germany. Inorganic Chemistry and Center for Nanointegration University of Duisburg-Essen Essen Germany. CAM-D Technologies Essen Germany. Institute for Bioinformatics and Chemoinformatics Westphalian University of Applied Sciences Recklinghausen Germany. Institute for Bioinformatics and Chemoinformatics Westphalian University of Applied Sciences Recklinghausen Germany. achim.zielesny@w-hs.de. Leiden University Leiden Netherlands. j.fraaije@chem.leidenuniv.nl. Culgi BV Berlin Germany. Physikalische Chemie III TU Dortmund 44227 Dortmund Germany. stefan.kast@tu-dortmund.de. Centre for Molecular Informatics Department of Chemistry University of Cambridge Lensfield Road Cambridge CB2 1EW United Kingdom. kcb27@cam.ac.uk. Centre for Molecular Informatics Department of Chemistry

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Novel neutralizing monoclonal antibodies protect rodents against lethal filovirus challenges

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Trials in Vaccinology 2014年第1期3卷 89-94页

作者： Marceau, Caleb D. Negi, Surendra S. Hernandez, Humberto Callison, Julie Marzi, Andrea Borisevich, Viktoriya Braun, Werner Berry, Jody Feldmann, Heinz Rockx, Barry Laboratory of Virology Division of Intramural Research NIAID Hamilton MT United States National Institutes of Health Undergraduate Scholarship Program (NIH-UGSP) United States Department of Pathology University of Texas Medical Branch Galveston TX 77555-0610 301 University Boulevard United States Department of Microbiology and Immunology University of Texas Medical Branch Galveston TX United States Sealy Center for Vaccine Development University of Texas Medical Branch Galveston TX United States Institute for Human Infections and Immunity University of Texas Medical Branch Galveston TX United States Sealy Center for Structural Biology and Molecular Biophysics University of Texas Medical Branch Galveston TX United States BD Biosciences San Diego CA United States Department of Microbiology and Immunology Stanford University United States

Filoviruses are the causative agents of lethal hemorrhagic fever in human and non-human primates (NHP). The family of Filoviridae is composed of three genera, Ebolavirus, Marburgvirus and Cuevavirus. There are currently no approved vaccines or antiviral therapeutics for the treatment of filovirus infections in humans. Passive transfer of neutralizing antibodies targeting the Ebola virus (EBOV) glycoprotein (GP) has proven effective in protecting mice, guinea pigs and NHP from lethal challenges with EBOV. In this study, we generated two neutralizing monoclonal antibodies (MAbs), termed S9 and M4 that recognize the GP of EBOV or multiple strains of Marburg virus (MARV), respectively. We characterized the putative binding site of S9 as a linear epitope on the glycan cap of the GP₁ subunit of the EBOV-GP. The M4 antibody recognizes an unknown conformational epitope on MARV-GP. Additionally, we demonstrated the post-exposure protection potential of these antibodies in both the mouse and guinea pig models of filovirus infection. These data indicate that MAbs S9 and M4 would be good candidates for inclusion in an antibody cocktail for the treatment of filovirus infections. © 2014 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license.

关键词： Animal model Filovirus Neutralizing antibody Prophylaxis

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Proceedings of the Frontiers of Retrovirology Conference 2016

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Retrovirology 2016年第1期13卷 1-40页

作者： Irena Zurnic Sylvia Hütter Nicole Stanke Tobias Kern Fabian Lindel Gesche Gerresheim Martin Hamann Erik Müllers Dirk Lindemann Ute Lehmann Juliane Reh Paul Lesbats Peter Cherepanov Melanie Mann Erik Serrao Alan Engelman Claire Da Silva Santos Kevin Tartour Andrea Cimarelli Rya Burdick Jianbo Chen Jaya Sastri Wei-Shau Hu Vinay Pathak Oliver T. Keppler Patrícia de Sousa-Pereira Hanna-Mari Baldauf Marcel Stern Karine Pradeau Sylvia Eiler Nicolas Levy Marc Ruff Sarah Lennon Sarah Cianferani Stéphane Emiliani Vincent Parissi Sylvie Rato Miguel Munoz Angela Ciuffi Antonio Rausell Amalio Telenti Alexander Zhyvoloup Ian Anderson Chen- Hsuin Lee Ariberto Fassati Anat Melamed Delphine Planas Petronela Ancuta Yuwei Zhang Huicheng Chen Annie Bernier Annie Gosselin Janos Kriston-Vizi Robin Ketteler Andy Merritt Charles Bangham Jocelyn Turpin Anthony Rodari Benoit Van Driessche Mathilde Galais Nadége Delacourt Sylvain Fauquenoy Caroline Vanhulle Anna Kula Carine Van Lint Ernst J. Wolvetang Arsène Burny Olivier Rohr Thijs van Montfort Renee van der Sluis Ben Berkhout Dave Speijer Gang Wang Na Zhao Atze T. Das Mirte Scherpenisse Bo Meng Andrzej Rutkowski Lars Dölken Andrew Lever Neil Berry Claire Ham Neil Almond Hoi Ping Mok Nicholas Norton Axel Fun Jack Hirst Mark Wills Chris Hellmund Harriet Groom Thomas Schuster Benedikt Asbach Ralf Wagner Christine Gross Martina Kalmer Andrea K. Thoma-Kress Norbert Donhauser Sebastian Millen Sandra M. Müller-Schmucker Veit Wiesmann Thomas Wittenberg Jan Gettemans Minghua Li Shan-Lu Liu Eric O. Freed Janis Müller Jan Münch Simone Joas Clement Wesley Gnanadurai Edina Lump Christina M. Stürzel Daniel Sauter Frank Kirchhoff Katharina Mack Kathrin Starz Christina Stürzel Xaver Sewald Nasim Motamedi Pradeep Uchil Ruoxi Pi Christin Herrmann Walther Mothes Mark Ladinsky Pamela Bjorkman Jagadish Beloor Priti Kumar Thomas Murooka Thorsten Mempel Michael Brehm Dale Greiner Erica Parrish Nicholas F. Parrish Beatrice H. Hahn Frederic Bibollet-Ruche Ulrike Sauermann Katharina Töpfer Tina Schultheiss Chris Molecular Virology and Gene Therapy Molecular Medicine Leuven Belgium Molecular Virology Technical University Dresden Dresden Germany Center for Regenerative Therapies Dresden Dresden Germany Potsdam University Potsdam Germany The Francis Crick Institute London Great Britain Institute of Clinical and Molecular Virology Friedrich-Alexander-Universität Erlangen-Nuremberg Erlangen Germany Dana Farber Cancer Institute Boston MA United States CIRI Lyon France National Cancer Institute Frederick MD United States Virology Max von Pettenkofer-Institut LMU Munich Munich Germany Institute of Medical Virology University of Frankfurt Frankfurt a. M. Germany German Center for Infection Research Munich Germany Institute of Medical Virology University Hospital Frankfurt Frankfurt a. M. Germany CIBIO/InBIO University of Porto Vairão Portugal Faculty of Sciences University of Porto Porto Portugal Virology Max von Pettenkofer Institute LMU Munich Germany Institute for Medical Virology Frankfurt a. M. Germany Integrative structural Biology IGBMC Illkirch France Institut Pluridisciplinaire Hubert Curien Strasbourg France Institut Cochin Paris France CNRS UMR5234 MFP Lab Bordeaux France Associated International Laboratory (LIA) Microbiology and Immunology CNRS/Université de Bordeaux/Heinrich Pette Institute-Leibniz Institute for Experimental Virology Bordeaux/Hamburg France Institute of Microbiology University Hospital Center and University of Lausanne Lausanne Switzerland Imagine Institute Paris Descartes University Paris France J. Craig Venter Institute La Jolla CA United States Infection University College London London Great Britain Medicine Imperial College London Great Britain Microbiology & Infection University of Montreal Montreal Great Britain CRCHUM Montreal Canada University College London LMCB London Great Britain MRC Technology Centre for Therapeutic Discovery London Great Britain Section of Virology Department of Medicine Imperial Co

Oral presentationsSession 1: Entry & uncoatingO1 Host cell polo-like kinases (PLKs) promote early prototype foamy virus (PFV) replicationIrena Zurnic, Sylvia Hütter, Ute Lehmann, Nicole Stanke, Juliane Re... 详细信息

Oral presentations

Session 1: Entry & uncoating

O1 Host cell polo-like kinases (PLKs) promote early prototype foamy virus (PFV) replication

Irena Zurnic, Sylvia Hütter, Ute Lehmann, Nicole Stanke, Juliane Reh, Tobias Kern, Fabian Lindel, Gesche Gerresheim, Martin Hamann, Erik Müllers, Paul Lesbats, Peter Cherepanov, Erik Serrao, Alan Engelman, Dirk Lindemann

O2 A novel entry/uncoating assay reveals the presence of at least two species of viral capsids during synchronized HIV-1 infection

Claire Da Silva Santos, Kevin Tartour, Andrea Cimarelli

O3 Dynamics of nuclear envelope association and nuclear import of HIV-1 complexes

Rya Burdick, Jianbo Chen, Jaya Sastri, Wei-Shau Hu, Vinay Pathak

O4 Human papillomavirus protein E4 potently enhances the susceptibility to HIV infection

Oliver T. Keppler

Session 2: Reverse transcription & integration

O5 Structure and function of HIV-1 integrase post translational modifications

Karine Pradeau, Sylvia Eiler, Nicolas Levy, Sarah Lennon, Sarah Cianferani, Stéphane Emiliani, Marc Ruff

O6 Regulation of retroviral integration by RNA polymerase II associated factors and chromatin structure

Vincent Parissi

Session 3: Transcription and latency

O7 A novel single-cell analysis pipeline to identify specific biomarkers of HIV permissiveness

Sylvie Rato, Antonio Rausell, Miguel Munoz, Amalio Telenti, Angela Ciuffi

O8 A capsid-dependent integration program linking T cell activation to HIV-1 gene expression

Alexander Zhyvoloup, Anat Melamed, Ian Anderson, Delphine Planas, Janos Kriston-Vizi, Robin Ketteler, Chen-Hsuin Lee, Andy Merritt, Petronela Ancuta, Charles Bangham, Ariberto Fassati

O9 Characterisation of new RNA polymerase III and RNA polymerase II transcriptional promoters in the Bovine Leukemia Virus genome

Anthony Rodari, Benoit Van Driessche, Mathilde Galais, Nadége Delacourt, Sylv

关键词： Human Immunodeficiency Virus Infection Simian Immunodeficiency Virus Feline Immunodeficiency Virus Bovine Leukemia Virus Prototype Foamy Virus

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Recognition of self and altered self by T cells in autoimmunity and allergy

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Protein & Cell 2013年第1期4卷 8-16页

作者： Lei Yin Shaodong Dai Gina Clayton Wei Gao Yang Wang John Kappler Philippa Marrack Howard Hughes Medical Institute and Integrated Department of Immunology National Jewish HealthDenverCO 80206USA Integrated Department of Immunology National Jewish HealthDenverCO80206USA Program in Structural Biology and Biophysics University of Colorado DenverSchool of MedicineAuroraCO 80045USA Department of Biochemistry and Molecular Genetics University of Colorado DenverSchool of MedicineAuroraCO 80045USA

T cell recognition of foreign peptide antigen and toler-ance to self peptides is key to the proper function of the immune ***,in the thymus T cells that rec-ognize self MHC+self peptides are deleted and those with the potential to recognize self MHC+foreign pep-tides are selected to *** there are excep-tions to these *** and allergy are two of the most common immune diseases that can be related to recognition of *** genes work together to lead to *** those,particular MHC alleles are the most strongly associated,reflecting the key importance of MHC presentation of self peptides in autoimmunity.T cells specific for combinations of self MHC and self pep-tides may escape thymus deletion,and thus be able to drive autoimmunity,for several reasons:the relevant self peptide may be presented at low abundance in the thy-mus but at high level in particular peripheral tissues;the relevant self peptide may bind to MHC in an unusual register,not present in the thymus but apparent else-where;finally the relevant self peptide may be post translationally modified in a tissue specific *** some types of allergy,the peptide+MHC combination may also be fully derived from *** the combi-nation in question may be modified by the presence of other ligands,such as small drug molecules or metal *** these types of allergies may act like the post translationally modified peptides involved some types of autoimmunity.

关键词： altered self neoantigen antigen presenting T cell recognition autoimmunity allergy diabetes der-matitis drug hypersensitivity

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The newly emerged SARS-Like coronavirus HCoV-EMC also has an “Achilles’ heel”: current effective inhibitor targeting a 3C-like protease

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Protein & Cell 2013年第4期4卷 248-250页

作者： Zhilin Ren Liming Yan Ning Zhang Yu Guo Cheng Yang Zhiyong Lou Zihe Rao College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology Nankai UniversityTianjin 300071China Structural Biology Laboratory and MOE Laboratory of Protein Science School of Medicine and Life ScienceTsinghua UniversityBeijing 100084China National Laboratory of Macromolecules Institute of BiophysicsChinese Academy of ScienceBeijing 100101China Emerging Infection Disease Program High-throughput Molecular Drug Discovery CenterTianjin Joint Academy of Biomedicine and TechnologyTianjin 300457China

From the global outbreak of SARS-CoV caused infection disease in 2003,coronaviruses(CoVs)are known to be a great threat to the human ***,a new SARS-like coronavirus,human betacoronavirus 2c EMC/2012(HCoV-EMC),has been identified and the appearance of this new CoV raises concerns that a new spread of CoV may occurs in the *** solving the crystal structure of HCoV-EMC main protease with a wide-spectrum anti-CoV inhibitor N3,we confi rmed that that N3 blocks the function of HCoV-EMC main protease through a similar mechanism to other *** with the good pharmaceutical features,N3 is conceivable to be effective to HCoV-EMC and other CoVs appearing in the *** fi ndings make it convincing that CoVs will not be a threat to human health.

关键词： EMC SARS Together

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Structure and Dynamics of Oligonucleotides in the Gas Phase†

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Angewandte Chemie 2014年第2期127卷

作者： Annalisa Arcella Jens Dreyer Emiliano Ippoliti Ivan Ivani Guillem Portella Valérie Gabelica Paolo Carloni Modesto Orozco Institute for Research in Biomedicine (IRB Barcelona) Joint BSC‐CRG‐IRB Program on Computational Biology Barcelona (Spain) Computational Biophysics German Research School for Simulation Sciences and Institute for Advanced Simulation IAS‐5 Computational Biomedicine Forschungszentrum Jülich (Germany) Mass Spectrometry Laboratory Department of Chemistry University of Liège (Belgium) Univ. Bordeaux IECB ARNA Laboratory 33600 Pessac (France) Inserm U869 ARNA Laboratory 33000 Bordeaux (France) Institute for Neuroscience and Medicine INM‐9 Computational Biomedicine Forschungszentrum Jülich (Germany) Department of Biochemistry and Molecular Biology University of Barcelona (Spain)

By combining ion‐mobility mass spectrometry experiments with sub‐millisecond classical and ab initio molecular dynamics we fully characterized, for the first time, the dynamic ensemble of a model nucleic acid in the gas phase under electrospray ionization conditions. The studied oligonucleotide unfolds upon vaporization, loses memory of the solution structure, and explores true gas‐phase conformational space. Contrary to our original expectations, the oligonucleotide shows very rich dynamics in three different timescales (multi‐picosecond, nanosecond, and sub‐millisecond). The shorter timescale dynamics has a quantum mechanical nature and leads to changes in the covalent structure, whereas the other two are of classical origin. Overall, this study suggests that a re‐evaluation on our view of the physics of nucleic acids upon vaporization is needed.

关键词： Ab‐initio‐Rechnungen DNA Gasphase Massenspektrometrie Moleküldynamik

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