NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein
about
NMR derived model of GTPase effector domain (GED) self association: relevance to dynamin assemblyLocal order in the unfolded state: conformational biases and nearest neighbor interactionsFurther biochemical and kinetic characterization of human eukaryotic initiation factor 4HNatively unfolded proteins: a point where biology waits for physicsThe plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, binds its siderophore in the absence of the transmembrane barrel domainIntrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backboneNMR elucidation of early folding hierarchy in HIV-1 protease.Neighboring residue effects in terminally blocked dipeptides: implications for residual secondary structures in intrinsically unfolded/disordered proteins.Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues.Molecular Dynamics Simulations of 441 Two-Residue Peptides in Aqueous Solution: Conformational Preferences and Neighboring Residue Effects with the Amber ff99SB-ildn-NMR Force Field.Intrinsic backbone preferences are fully present in blocked amino acidsOrigin of the neighboring residue effect on peptide backbone conformation.Construction and comparison of the statistical coil states of unfolded and intrinsically disordered proteins from nearest-neighbor corrected conformational propensities of short peptides.Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: distributions of phi.Regulation of the cystic fibrosis transmembrane conductance regulator Cl- channel by its R domain.Statistical coil model of the unfolded state: resolving the reconciliation problem.Describing sequence-ensemble relationships for intrinsically disordered proteins.Local control of a disorder-order transition in 4E-BP1 underpins regulation of translation via eIF4E.NMR insights into folding and self-association of Plasmodium falciparum P2.Local structural preferences and dynamics restrictions in the urea-denatured state of SUMO-1: NMR characterization.NMR investigations of structural and dynamics features of natively unstructured drug peptide - salmon calcitonin: implication to rational design of potent sCT analogs.Populations of the three major backbone conformations in 19 amino acid dipeptides.The intrinsic conformational features of amino acids from a protein coil library and their applications in force field development.Intrinsically disordered proteins (IDPs) in trypanosomatids.Electrostatic screening and backbone preferences of amino acid residues in urea-denatured ubiquitin.Structural and dynamic characterization of an unfolded state of poplar apo-plastocyanin formed under nondenaturing conditions.Structural landscape of the proline-rich domain of Sos1 nucleotide exchange factorRegulation of cell division by intrinsically unstructured proteins: intrinsic flexibility, modularity, and signaling conduits.A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solutionOrigin of the change in solvation enthalpy of the peptide group when neighboring peptide groups are added.Biophysical characterization of intrinsically disordered proteins.Adsorption of fibronectin on salt-etched polyelectrolyte multilayers and its roles in mediating the adhesion and migration of vascular smooth muscle cells.The Proline/Glycine-Rich Region of the Biofilm Adhesion Protein Aap Forms an Extended Stalk that Resists Compaction.The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered proteinChange in backbone torsion angle distribution on protein folding.Structural consequences of site-directed mutagenesis in flexible protein domains: NMR characterization of the L(55,56)S mutant of RhoGDI.Equilibrium NMR studies of unfolded and partially folded proteins.
P2860
Q21560884-69AA4B1D-46E6-4CCC-B678-76085646558BQ26851842-A0F64599-1140-4C0C-8B6C-DC9208428D28Q28139473-AC8E5F82-EA44-4F58-BE39-C03A612BF9D1Q29616416-CFF326C6-8A71-4A58-855A-2BB8ABDB57DCQ30167969-0B54386B-8574-4B26-B1AC-3CA77DFA6316Q30322825-C3113C9F-9C46-4822-AEAD-14D7DE305208Q30332630-EE703B96-09F5-4AE6-90F9-98ECAD4789DAQ30358192-F1AF958A-23DA-42FF-8493-5E1CFD4D5047Q30372268-4CEBC35F-06E1-43C8-B6B6-34FCC2FB2BC7Q31025559-C33A4D97-EA48-4A6C-A85E-17BA2EFB9223Q31030110-4DD1756A-29A0-4AB6-AD7E-0C1C981AB72BQ31094215-8FE3B90E-3CAE-4278-AE13-3958400C9A2BQ31122664-6D0F1182-26CD-4424-B8F7-2C7B281E131DQ31140155-BB62E785-8A42-4B32-AB90-E64B4AF85B70Q32186098-9E360409-2293-4098-8321-B469C6DD0728Q33222591-86F7690A-6D04-4838-80F9-71391DEC66C8Q33818465-8ED751B9-0FA0-48C4-99D2-1A9BB9884D07Q34199867-33606977-031C-4A0A-B3CE-8003A052CBA0Q34261765-61333D60-7BBB-4BE9-95D7-11EA91769F98Q34452373-8DA83256-AC14-4FB1-BC39-1F879E0FEDDCQ34499176-0ED8EBAB-2579-4C00-8ED0-89E763B6861CQ34550065-D478ED51-C885-4D5A-91E1-93A7B99A1B1AQ34577841-35B3B724-4014-4B94-8D06-639804890502Q35228279-4EC1D8A9-D245-4889-9061-880EE78CBA8AQ36388139-63C60BA4-049E-4207-B918-E81DAB0D5866Q36640705-0D03A43D-A2C2-4546-837D-B7473CD3B907Q36736139-361CB603-7E82-4EE0-B0A3-014782CDCF38Q36967218-011FAD1B-00C8-4716-8841-2914291F419FQ36986382-D32EFCEF-6CDA-436A-A927-D2FFF2499CF9Q37117595-808E6378-4306-45DC-A327-AEE2039CCBA0Q37375367-C79CEEA9-4EBA-493A-8F57-81580C225CDBQ38950442-D8F664AF-755B-46F5-A8EB-BB2D657BB031Q40434276-13525EA1-E0E0-4184-9512-91AE4B6C8784Q42123533-100439B6-2EFC-4154-A399-D8B71F9E73E0Q42847690-48A8D411-3126-4A53-9A9C-710DDA4B6862Q43572388-63C2280C-7C44-4F2F-96F6-212394DCE039Q46162800-CC90FF31-AA40-4A32-9D32-DBE0DEB682CA
P2860
NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein
description
article
@en
im November 1997 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в листопаді 1997
@uk
name
NMR analysis of main-chain con ...... ed fibronectin-binding protein
@en
NMR analysis of main-chain con ...... ed fibronectin-binding protein
@nl
type
label
NMR analysis of main-chain con ...... ed fibronectin-binding protein
@en
NMR analysis of main-chain con ...... ed fibronectin-binding protein
@nl
prefLabel
NMR analysis of main-chain con ...... ed fibronectin-binding protein
@en
NMR analysis of main-chain con ...... ed fibronectin-binding protein
@nl
P2093
P356
P1476
NMR analysis of main-chain con ...... ed fibronectin-binding protein
@en
P2093
Christopher J Penkett
Danuta E Mossakowska
Diane L McBay
Julia Hubbard
Lorna J Smith
Richard A.G Smith
P304
P356
10.1006/JMBI.1997.1369
P407
P577
1997-11-01T00:00:00Z