Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins.
暂无分享,去创建一个
[1] A. Fersht,et al. Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain , 2008, Proceedings of the National Academy of Sciences.
[2] H. Dyson,et al. Coupling of folding and binding for unstructured proteins. , 2002, Current opinion in structural biology.
[3] Sonia Longhi,et al. Intrinsic disorder in measles virus nucleocapsids , 2011, Proceedings of the National Academy of Sciences.
[4] Martin Blackledge,et al. NMR characterization of long-range order in intrinsically disordered proteins. , 2010, Journal of the American Chemical Society.
[5] P. Tompa. Intrinsically unstructured proteins. , 2002, Trends in biochemical sciences.
[6] Martin Blackledge,et al. Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution. , 2012, Journal of the American Chemical Society.
[7] Abhishek K. Jha,et al. Statistical coil model of the unfolded state: resolving the reconciliation problem. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[8] Martin Blackledge,et al. Sequence-specific mapping of the interaction between urea and unfolded ubiquitin from ensemble analysis of NMR and small angle scattering data. , 2012, Journal of the American Chemical Society.
[9] D. Eliezer,et al. Biophysical characterization of intrinsically disordered proteins. , 2009, Current opinion in structural biology.
[10] Martin von Bergen,et al. Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation. , 2007, Journal of the American Chemical Society.
[11] Pau Bernadó,et al. A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[12] Jie-rong Huang,et al. Ensemble calculations of unstructured proteins constrained by RDC and PRE data: a case study of urea-denatured ubiquitin. , 2010, Journal of the American Chemical Society.
[13] Martin Blackledge,et al. Amino acid bulkiness defines the local conformations and dynamics of natively unfolded alpha-synuclein and tau. , 2007, Journal of the American Chemical Society.
[14] Martin Tollinger,et al. Calculation of residual dipolar couplings from disordered state ensembles using local alignment. , 2008, Journal of the American Chemical Society.
[15] Martin Blackledge,et al. Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein. , 2008, Journal of the American Chemical Society.
[16] Céline Charavay,et al. Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables , 2012, Bioinform..
[17] S. Grzesiek,et al. Residual dipolar couplings measured in unfolded proteins are sensitive to amino-acid-specific geometries as well as local conformational sampling. , 2012, Biochemical Society transactions.
[18] Martin Blackledge,et al. Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings. , 2007, Journal of the American Chemical Society.
[19] C. Dobson,et al. Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea. , 1997, Biochemistry.
[20] M. Blackledge,et al. Defining long-range order and local disorder in native alpha-synuclein using residual dipolar couplings. , 2005, Journal of the American Chemical Society.
[21] Martin Blackledge,et al. Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings. , 2009, Journal of the American Chemical Society.
[22] Christian Griesinger,et al. Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings. , 2009, Structure.
[23] Gerard J A Kroon,et al. Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings. , 2004, Journal of molecular biology.
[24] Martin Blackledge,et al. Conformational distributions of unfolded polypeptides from novel NMR techniques. , 2008, The Journal of chemical physics.
[25] H. Dyson,et al. Intrinsically unstructured proteins and their functions , 2005, Nature Reviews Molecular Cell Biology.
[26] S. Grzesiek,et al. Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings. , 2010, Journal of the American Chemical Society.
[27] D. Shortle,et al. Persistence of Native-Like Topology in a Denatured Protein in 8 M Urea , 2001, Science.
[28] Luca Mollica,et al. Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy. , 2012, Molecular bioSystems.
[29] Joseph A Marsh,et al. Improved structural characterizations of the drkN SH3 domain unfolded state suggest a compact ensemble with native-like and non-native structure. , 2007, Journal of molecular biology.
[30] Arto Annila,et al. On the origin of residual dipolar couplings from denatured proteins. , 2003, Journal of the American Chemical Society.
[31] V. Uversky. Natively unfolded proteins: A point where biology waits for physics , 2002, Protein science : a publication of the Protein Society.
[32] J M Thornton,et al. Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. , 1996, Journal of molecular biology.
[33] L. Iakoucheva,et al. Intrinsic Disorder and Protein Function , 2002 .
[34] F. Poulsen,et al. Short-range, long-range and transition state interactions in the denatured state of ACBP from residual dipolar couplings. , 2004, Journal of molecular biology.