Protein chemical shifts arising from alpha-helices and beta-sheets depend on solvent exposure.
about
Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free waterNMR evidence for forming highly populated helical conformations in the partially folded hNck2 SH3 domain.Neighboring residue effects in terminally blocked dipeptides: implications for residual secondary structures in intrinsically unfolded/disordered proteins.Protein structural information derived from NMR chemical shift with the neural network program TALOS-N.Relationship between chemical shift value and accessible surface area for all amino acid atoms.Chemical shift prediction for protein structure calculation and quality assessment using an optimally parameterized force field.Accessible surface area from NMR chemical shifts.NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120 in methanol and water.Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix proteinA comprehensive library of blocked dipeptides reveals intrinsic backbone conformational propensities of unfolded proteins.Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme.Unusual molecular mechanism behind the thermal response of polypeptoids in aqueous solutions.Electrostatic screening and backbone preferences of amino acid residues in urea-denatured ubiquitin.Building native protein conformation from NMR backbone chemical shifts using Monte Carlo fragment assemblyElectron spin density on the axial His ligand of high-spin and low-spin nitrophorin 2 probed by heteronuclear NMR spectroscopyPressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH2.Conformational properties of the unfolded state of Im7 in nondenaturing conditionsConformational dynamics is more important than helical propensity for the folding of the all α-helical protein Im7.13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues.Insights into the molecular flexibility of θ-defensins by NMR relaxation analysis.A de Novo-Designed Monomeric, Compact Three-Helix-Bundle Protein on a Carbohydrate Template.MgF3- and AlF4- transition state analogue complexes of yeast phosphoglycerate kinase.Conformational distributions of denatured and unstructured proteins are similar to those of 20 × 20 blocked dipeptides.Measurement of Structural Restraints
P2860
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P2860
Protein chemical shifts arising from alpha-helices and beta-sheets depend on solvent exposure.
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Protein chemical shifts arisin ...... ts depend on solvent exposure.
@ast
Protein chemical shifts arisin ...... ts depend on solvent exposure.
@en
type
label
Protein chemical shifts arisin ...... ts depend on solvent exposure.
@ast
Protein chemical shifts arisin ...... ts depend on solvent exposure.
@en
prefLabel
Protein chemical shifts arisin ...... ts depend on solvent exposure.
@ast
Protein chemical shifts arisin ...... ts depend on solvent exposure.
@en
P2093
P2860
P356
P1476
Protein chemical shifts arisin ...... ts depend on solvent exposure.
@en
P2093
Darko Kocjan
Franc Avbelj
Robert L Baldwin
P2860
P304
17394-17397
P356
10.1073/PNAS.0407969101
P407
P577
2004-12-01T00:00:00Z