NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
about
X-ray Crystallographic and Solution State Nuclear Magnetic Resonance Spectroscopic Investigations of NADP + Binding to Ferredoxin NADP Reductase from Pseudomonas aeruginosa † , ‡The WW domain of dystrophin requires EF-hands region to interact with beta-dystroglycanThe unfolded state of the villin headpiece helical subdomain: computational studies of the role of locally stabilized structureNMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiationDirect detection of transient alpha-helical states in islet amyloid polypeptideConformations of a Metastable SH3 Domain Characterized by smFRET and an Excluded-Volume Polymer ModelParamagnetic relaxation enhancements in unfolded proteins: theory and application to drkN SH3 domain.Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri TipPosttransition state desolvation of the hydrophobic core of the src-SH3 protein domainProtein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapseMolecular dynamics simulations of a highly charged peptide from an SH3 domain: possible sequence-function relationship.Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain.Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathwaySite-specific contributions to the pH dependence of protein stabilityBackbone dynamics of the monomeric lambda repressor denatured state ensemble under nondenaturing conditions.Engineering a signal transduction mechanism for protein-based biosensors.Binding of the MLL PHD3 finger to histone H3K4me3 is required for MLL-dependent gene transcription.Propensities of aromatic amino acids versus leucine and proline to induce residual structure in the denatured-state ensemble of iso-1-cytochrome c.Folding pathway of a lattice model for proteins.Manifestations of native topology in the denatured state ensemble of Rhodopseudomonas palustris cytochrome c'.Measurement of bond vector orientations in invisible excited states of proteins.15N backbone dynamics of the S-peptide from ribonuclease A in its free and S-protein bound forms: toward a site-specific analysis of entropy changes upon foldingGroEL-mediated protein folding: making the impossible, possible.Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.Thermodynamics of protein denatured states.Hsp70 biases the folding pathways of client proteins.Fluorescence characterization of denatured proteins.Residual structure within the disordered C-terminal segment of p21(Waf1/Cip1/Sdi1) and its implications for molecular recognition.Localized thermodynamic coupling between hydrogen bonding and microenvironment polarity substantially stabilizes proteins.NMR assignments and histone specificity of the ING2 PHD fingerIntrinsically disordered proteins: from sequence and conformational properties toward drug discovery.Measuring 1HN temperature coefficients in invisible protein states by relaxation dispersion NMR spectroscopy.Beyond molecular beacons: optical sensors based on the binding-induced folding of proteins and polypeptides.Interconnection of salt-induced hydrophobic compaction and secondary structure formation depends on solution conditions: revisiting early events of protein folding at single molecule resolution.Tryptophan stabilizes His-heme loops in the denatured state only when it is near a loop endFolding transition-state and denatured-state ensembles of FSD-1 from folding and unfolding simulations.The contribution of the residues from the main hydrophobic core of ribonuclease A to its pressure-folding transition state.Equilibrium NMR studies of unfolded and partially folded proteins.Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Under-folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis.
P2860
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P2860
NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
description
1997 nî lūn-bûn
@nan
1997 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
NMR studies of unfolded states ...... ion and denaturing conditions.
@ast
NMR studies of unfolded states ...... ion and denaturing conditions.
@en
type
label
NMR studies of unfolded states ...... ion and denaturing conditions.
@ast
NMR studies of unfolded states ...... ion and denaturing conditions.
@en
prefLabel
NMR studies of unfolded states ...... ion and denaturing conditions.
@ast
NMR studies of unfolded states ...... ion and denaturing conditions.
@en
P356
P1433
P1476
NMR studies of unfolded states ...... ion and denaturing conditions.
@en
P2093
Forman-Kay JD
P304
P356
10.1021/BI9627626
P407
P577
1997-04-01T00:00:00Z