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Classification of Intrinsically Disordered Regions and Proteins

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        Rapid planetesimal formation in turbulent circumstellar discs

        The initial stages of planet formation in circumstellar gas discs proceed via dust grains that collide and build up larger and larger bodies (Safronov 1969). How this process continues from metre-sized boulders to kilometre-scale planetesimals is a major unsolved problem (Dominik et al. 2007): boulders stick together poorly (Benz 2000), and spiral into the protostar in a few hundred orbits due to a head wind from the slower rotating gas (Weidenschilling 1977). Gravitational collapse of the solid component has been suggested to overcome this barrier (Safronov 1969, Goldreich & Ward 1973, Youdin & Shu 2002). Even low levels of turbulence, however, inhibit sedimentation of solids to a sufficiently dense midplane layer (Weidenschilling & Cuzzi 1993, Dominik et al. 2007), but turbulence must be present to explain observed gas accretion in protostellar discs (Hartmann 1998). Here we report the discovery of efficient gravitational collapse of boulders in locally overdense regions in the midplane. The boulders concentrate initially in transient high pressures in the turbulent gas (Johansen, Klahr, & Henning 2006), and these concentrations are augmented a further order of magnitude by a streaming instability (Youdin & Goodman 2005, Johansen, Henning, & Klahr 2006, Johansen & Youdin 2007) driven by the relative flow of gas and solids. We find that gravitationally bound clusters form with masses comparable to dwarf planets and containing a distribution of boulder sizes. Gravitational collapse happens much faster than radial drift, offering a possible path to planetesimal formation in accreting circumstellar discs.
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          Chromatin modifications and their function.

          The surface of nucleosomes is studded with a multiplicity of modifications. At least eight different classes have been characterized to date and many different sites have been identified for each class. Operationally, modifications function either by disrupting chromatin contacts or by affecting the recruitment of nonhistone proteins to chromatin. Their presence on histones can dictate the higher-order chromatin structure in which DNA is packaged and can orchestrate the ordered recruitment of enzyme complexes to manipulate DNA. In this way, histone modifications have the potential to influence many fundamental biological processes, some of which may be epigenetically inherited.

            Author and article information

            []MRC Laboratory of Molecular Biology , Francis Crick Avenue, Cambridge CB2 0QH, United Kingdom
            []Centre for Molecular and Biomolecular Informatics, Radboud University Medical Centre , 6500 HB Nijmegen, The Netherlands
            [§ ]Department of Cell Biology, Microbiology, and Molecular Biology, University of South Florida , 3720 Spectrum Boulevard, Suite 321, Tampa, Florida 33612, United States
            []Department of Biochemistry and Molecular Biology, Indiana University School of Medicine , Indianapolis, Indiana 46202, United States
            []MTA-DE Momentum Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen , H-4032 Debrecen, Nagyerdei krt 98, Hungary
            [# ]Department of Computer Science, University of Bristol , The Merchant Venturers Building, Bristol BS8 1UB, United Kingdom
            []Department of Biochemistry and Molecular Biology, Centre for High-Throughput Biology, University of British Columbia , Vancouver, British Columbia V6T 1Z4, Canada
            []Bioinformatics Group, Department of Computer Science, University College London , London, WC1E 6BT, United Kingdom
            Terrence Donnelly Centre for Cellular and Biomolecular Research, Department of Molecular Genetics, and Department of Computer Science, University of Toronto , Toronto, Ontario M5S 3E1, Canada
            []Department of Structural Biology, St. Jude Children’s Research Hospital , Memphis, Tennessee 38105, United States
            [& ]Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis , St. Louis, Missouri 63130, United States
            [@ ]VIB Department of Structural Biology, Vrije Universiteit Brussel , Brussels, Belgium
            [$ ]Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences , Budapest, Hungary
            [% ]Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida , Tampa, Florida 33612, United States
            []Institute for Biological Instrumentation, Russian Academy of Sciences , Pushchino, Moscow Region, Russia
            []Department of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States
            Author notes
            Chem Rev
            Chem. Rev
            Chemical Reviews
            American Chemical Society
            29 April 2015
            29 April 2014
            09 July 2014
            : 114
            : 13 , 2014 Intrinsically Disordered Proteins (IDPs)
            : 6589-6631
            24773235 4095912 10.1021/cr400525m
            Copyright © 2014 American Chemical Society

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