Buried and accessible surface area control intrinsic protein flexibility.

[1]  W. Kauzmann Some factors in the interpretation of protein denaturation. , 1959, Advances in protein chemistry.

[2]  C. Chothia,et al.  Hydrophobic bonding and accessible surface area in proteins , 1974, Nature.

[3]  C. Chothia Structural invariants in protein folding , 1975, Nature.

[4]  J. Janin,et al.  Surface area of globular proteins. , 1976, Journal of molecular biology.

[5]  D. Teller Accessible area, packing volumes and interaction surfaces of globular proteins , 1976, Nature.

[6]  M. Levitt Conformational preferences of amino acids in globular proteins. , 1978, Biochemistry.

[7]  W A Hendrickson,et al.  Influence of solvent accessibility and intermolecular contacts on atomic mobilities in hemerythrins. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[8]  Cyrus Chothia,et al.  The accessible surface area and stability of oligomeric proteins , 1987, Nature.

[9]  A M Lesk,et al.  Interior and surface of monomeric proteins. , 1987, Journal of molecular biology.

[10]  P. Wolynes,et al.  The energy landscapes and motions of proteins. , 1991, Science.

[11]  Collaborative Computational,et al.  The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.

[12]  A. Lesk,et al.  Structural mechanisms for domain movements in proteins. , 1994, Biochemistry.

[13]  P Argos,et al.  The role of side-chain hydrogen bonds in the formation and stabilization of secondary structure in soluble proteins. , 1994, Journal of molecular biology.

[14]  M. Vihinen,et al.  Accuracy of protein flexibility predictions , 1994, Proteins.

[15]  J. Thornton,et al.  Satisfying hydrogen bonding potential in proteins. , 1994, Journal of molecular biology.

[16]  C. Dobson,et al.  Structural determinants of protein dynamics: analysis of 15N NMR relaxation measurements for main-chain and side-chain nuclei of hen egg white lysozyme. , 1995, Biochemistry.

[17]  A G Murzin,et al.  SCOP: a structural classification of proteins database for the investigation of sequences and structures. , 1995, Journal of molecular biology.

[18]  P. Argos,et al.  Knowledge‐based protein secondary structure assignment , 1995, Proteins.

[19]  P Argos,et al.  Correlation between side chain mobility and conformation in protein structures. , 1997, Protein engineering.

[20]  R. Abseher,et al.  Essential spaces defined by NMR structure ensembles and molecular dynamics simulation show significant overlap , 1998, Proteins.

[21]  D. Covell,et al.  Correlation between native-state hydrogen exchange and cooperative residue fluctuations from a simple model. , 1998, Biochemistry.

[22]  M. Philippopoulos,et al.  Exploring the dynamic information content of a protein NMR structure: Comparison of a molecular dynamics simulation with the NMR and X‐ray structures of Escherichia coli ribonuclease HI , 1999, Proteins.

[23]  H. Dyson,et al.  Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. , 1999, Journal of molecular biology.

[24]  R. Nussinov,et al.  Folding funnels, binding funnels, and protein function , 1999, Protein science : a publication of the Protein Society.

[25]  C. Chothia,et al.  The Packing Density in Proteins: Standard Radii and Volumes , 1999 .

[26]  M. Karplus,et al.  Native proteins are surface-molten solids: application of the Lindemann criterion for the solid versus liquid state. , 1999, Journal of molecular biology.

[27]  V. Uversky,et al.  Why are “natively unfolded” proteins unstructured under physiologic conditions? , 2000, Proteins.

[28]  Y. Sanejouand,et al.  Conformational change of proteins arising from normal mode calculations. , 2001, Protein engineering.

[29]  K A Dill,et al.  Are proteins well-packed? , 2001, Biophysical journal.

[30]  Y. Yamagata,et al.  Contribution of polar groups in the interior of a protein to the conformational stability. , 2001, Biochemistry.

[31]  Christopher J. Oldfield,et al.  Intrinsically disordered protein. , 2001, Journal of molecular graphics & modelling.

[32]  B. Halle,et al.  Flexibility and packing in proteins , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[33]  Rafael Brüschweiler,et al.  Contact model for the prediction of NMR N-H order parameters in globular proteins. , 2002, Journal of the American Chemical Society.

[34]  George I Makhatadze,et al.  Thermodynamic consequences of burial of polar and non-polar amino acid residues in the protein interior. , 2002, Journal of molecular biology.

[35]  C. A. Andersen,et al.  Continuum secondary structure captures protein flexibility. , 2002, Structure.

[36]  Karsten Suhre,et al.  ElNémo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement , 2004, Nucleic Acids Res..

[37]  Igor Polikarpov,et al.  Average protein density is a molecular‐weight‐dependent function , 2004, Protein science : a publication of the Protein Society.

[38]  Eran Eyal,et al.  Importance of solvent accessibility and contact surfaces in modeling side‐chain conformations in proteins , 2004, J. Comput. Chem..

[39]  M. Y. Lobanov,et al.  To be folded or to be unfolded? , 2004, Protein science : a publication of the Protein Society.

[40]  Ruth Nussinov,et al.  Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers. , 2004, Journal of molecular biology.

[41]  P. Tompa,et al.  The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. , 2005, Journal of molecular biology.

[42]  Miron Livny,et al.  RECOORD: A recalculated coordinate database of 500+ proteins from the PDB using restraints from the BioMagResBank , 2005, Proteins.

[43]  I. Bahar,et al.  Coarse-grained normal mode analysis in structural biology. , 2005, Current opinion in structural biology.

[44]  J. Beckmann,et al.  FoldIndex©: a simple tool to predict whether a given protein sequence is intrinsically unfolded , 2005 .

[45]  P. Radivojac,et al.  PROTEINS: Structure, Function, and Bioinformatics Suppl 7:176–182 (2005) Exploiting Heterogeneous Sequence Properties Improves Prediction of Protein Disorder , 2022 .

[46]  Jaime Prilusky,et al.  FoldIndex copyright: a simple tool to predict whether a given protein sequence is intrinsically unfolded , 2005, Bioinform..

[47]  David S Wishart,et al.  A simple method to predict protein flexibility using secondary chemical shifts. , 2005, Journal of the American Chemical Society.

[48]  B. Rost,et al.  Protein flexibility and rigidity predicted from sequence , 2005, Proteins.

[49]  Zoran Obradovic,et al.  Length-dependent prediction of protein intrinsic disorder , 2006, BMC Bioinformatics.

[50]  Michail Yu. Lobanov,et al.  Prediction of Amyloidogenic and Disordered Regions in Protein Chains , 2006, PLoS Comput. Biol..

[51]  C. Chennubhotla,et al.  Insights into equilibrium dynamics of proteins from comparison of NMR and X-ray data with computational predictions. , 2007, Structure.

[52]  D. Kern,et al.  Dynamic personalities of proteins , 2007, Nature.

[53]  Emmanuel D Levy,et al.  PiQSi: protein quaternary structure investigation. , 2007, Structure.

[54]  P. Chacón,et al.  Thorough validation of protein normal mode analysis: a comparative study with essential dynamics. , 2007, Structure.

[55]  K. Henrick,et al.  Inference of macromolecular assemblies from crystalline state. , 2007, Journal of molecular biology.

[56]  M. Seibert,et al.  On the precision of calculated solvent-accessible surface areas. , 2007, Acta crystallographica. Section D, Biological crystallography.

[57]  N. S. Bogatyreva,et al.  [Radius of gyration is indicator of compactness of protein structure]. , 2008, Molekuliarnaia biologiia.

[58]  O. Galzitskaya,et al.  More compact protein globules exhibit slower folding rates , 2007, Proteins.

[59]  S. Teichmann,et al.  Assembly reflects evolution of protein complexes , 2008, Nature.

[60]  O. V. Galzitskaya,et al.  Radius of gyration as an indicator of protein structure compactness , 2008, Molecular Biology.

[61]  M. Sternberg,et al.  Insights into protein flexibility: The relationship between normal modes and conformational change upon protein–protein docking , 2008, Proceedings of the National Academy of Sciences.

[62]  Oxana V. Galzitskaya,et al.  Coupling between Properties of the Protein Shape and the Rate of Protein Folding , 2009, PloS one.

[63]  M. Gerstein,et al.  Relating protein conformational changes to packing efficiency and disorder , 2009, Protein science : a publication of the Protein Society.

[64]  Lukasz Kurgan,et al.  On the relation between residue flexibility and local solvent accessibility in proteins , 2009, Proteins.

[65]  Xin Deng,et al.  PreDisorder: ab initio sequence-based prediction of protein disordered regions , 2009, BMC Bioinformatics.

[66]  J. Marsh,et al.  Sequence determinants of compaction in intrinsically disordered proteins. , 2010, Biophysical journal.

[67]  L. Reymond,et al.  Charge interactions can dominate the dimensions of intrinsically disordered proteins , 2010, Proceedings of the National Academy of Sciences.

[68]  D. Svergun,et al.  Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation. , 2010, Biophysical journal.

[69]  E. Levy A simple definition of structural regions in proteins and its use in analyzing interface evolution. , 2010, Journal of molecular biology.

[70]  J. Marsh,et al.  Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators. , 2010, Structure.

[71]  L. Reymond,et al.  Charge interactions can dominate the dimensions of intrinsically disordered proteins , 2010, Proceedings of the National Academy of Sciences.

[72]  Michael Levitt,et al.  Super-resolution biomolecular crystallography with low-resolution data , 2010, Nature.

[73]  Caitlin L. Chicoine,et al.  Net charge per residue modulates conformational ensembles of intrinsically disordered proteins , 2010, Proceedings of the National Academy of Sciences.

[74]  Ugo Bastolla,et al.  Torsional network model: normal modes in torsion angle space better correlate with conformation changes in proteins. , 2010, Physical review letters.

[75]  Modesto Orozco,et al.  MoDEL (Molecular Dynamics Extended Library): a database of atomistic molecular dynamics trajectories. , 2010, Structure.

[76]  H. Gohlke,et al.  Large‐scale comparison of protein essential dynamics from molecular dynamics simulations and coarse‐grained normal mode analyses , 2010, Proteins.

[77]  O. Galzitskaya,et al.  Accessible Surfaces of Beta Proteins Increase with Increasing Protein Molecular Mass More Rapidly than Those of Other Proteins , 2011, PloS one.

[78]  Sarah A. Teichmann,et al.  Relative Solvent Accessible Surface Area Predicts Protein Conformational Changes upon Binding , 2011, Structure.

[79]  Collin M. Stultz,et al.  Protein Structure along the Order–Disorder Continuum , 2011, Journal of the American Chemical Society.

[80]  Silvio C. E. Tosatto,et al.  ESpritz: accurate and fast prediction of protein disorder , 2012, Bioinform..

[81]  S. Teichmann,et al.  Probing the diverse landscape of protein flexibility and binding. , 2012, Current opinion in structural biology.

[82]  K. Dill,et al.  The Protein-Folding Problem, 50 Years On , 2012, Science.

[83]  Monika Fuxreiter,et al.  Fuzziness: linking regulation to protein dynamics. , 2012, Molecular bioSystems.

[84]  Luca Mollica,et al.  Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy. , 2012, Molecular bioSystems.

[85]  G. Vriend,et al.  Exploring Protein Dynamics Space: The Dynasome as the Missing Link between Protein Structure and Function , 2012, PloS one.

[86]  Joseph A Marsh,et al.  Ensemble modeling of protein disordered states: Experimental restraint contributions and validation , 2011, Proteins.

[87]  S. Teichmann,et al.  Protein Complexes Are under Evolutionary Selection to Assemble via Ordered Pathways , 2013, Cell.

[88]  V. Uversky Intrinsically Disordered Proteins , 2014 .