Equilibrium NMR studies of unfolded and partially folded proteins. - Wikidata - wikimedia - TriplyDB

Equilibrium NMR studies of unfolded and partially folded proteins.

Equilibrium NMR studies of unfolded and partially folded proteins.

http://www.wikidata.org/entity/Q46162800

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Folding very short peptides using molecular dynamics Classification of intrinsically disordered regions and proteins Rotamer strain as a determinant of protein structural specificity Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution De novo designed cyclic-peptide heme complexes Implementation of a k/k0 Method to Identify Long-Range Structure in Transition States during Conformational Folding/Unfolding of Proteins High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment Evolutionary Pareto-optimization of stably folding peptides Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy.Assigning backbone NMR resonances for full length tau isoforms: efficient compromise between manual assignments and reduced dimensionality NMR characterization of the near native and unfolded states of the PTB domain of Dok1: alternate conformations and residual clusters Sparsely populated folding intermediates of the Fyn SH3 domain: matching native-centric essential dynamics and experiment Characterization of the structure and dynamics of a near-native equilibrium intermediate in the unfolding pathway of an all beta-barrel protein.The expanded FindCore method for identification of a core atom set for assessment of protein structure prediction.Molecular dynamics simulations of the native and partially folded states of ubiquitin: influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics.Molecular Simulations Find Stable Structures in Fragments of Protein G.Resonance assignment of disordered protein with repetitive and overlapping sequence using combinatorial approach reveals initial structural propensities and local restrictions in the denatured state.Protein intrinsic disorder in Arabidopsis NAC transcription factors: transcriptional activation by ANAC013 and ANAC046 and their interactions with RCD1.The tooth enamel protein, porcine amelogenin, is an intrinsically disordered protein with an extended molecular configuration in the monomeric form.NMR characterization of partially folded and unfolded conformational ensembles of proteins.Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein Disorder predictors also predict backbone dynamics for a family of disordered proteins Primary folding dynamics of sperm whale apomyoglobin: core formation Guanidine-HCl dependent structural unfolding of M-crystallin: fluctuating native state like topologies and intermolecular association.The SCHOOL of nature: III. From mechanistic understanding to novel therapies Probing the self-association, intermolecular contacts, and folding propensity of amelogenin.L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment.Conformational properties of native sperm whale apomyoglobin in solution.Native-state hydrogen-exchange studies of a fragment complex can provide structural information about the isolated fragments.Dynamical characterization of residual and non-native structures in a partially folded protein by (15)N NMR relaxation using a model based on a distribution of correlation times.Structural and dynamic characterization of an unfolded state of poplar apo-plastocyanin formed under nondenaturing conditions.Order-disorder-order transitions mediate the activation of cholera toxin.Hydration dynamics in a partially denatured ensemble of the globular protein human alpha-lactalbumin investigated with molecular dynamics simulations.Probing the instabilities in the dynamics of helical fragments from mouse PrPC.Revisiting the conundrum of trehalose stabilization.How cooperative are protein folding and unfolding transitions?A measure of conformational entropy change during thermal protein unfolding using neutron spectroscopy.The SCHOOL of nature: II. Protein order, disorder and oligomericity in transmembrane signaling.Unusual biophysics of immune signaling-related intrinsically disordered proteins.Charge-charge interactions influence the denatured state ensemble and contribute to protein stability.

P2860

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P2860

Equilibrium NMR studies of unfolded and partially folded proteins.

http://www.wikidata.org/entity/Q46162800

description

1998 nî lūn-bûn

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1998年の論文

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

@zh-my

1998年学术文章

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1998年學術文章

@yue

1998年學術文章

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name

Equilibrium NMR studies of unfolded and partially folded proteins.

@en

Equilibrium NMR studies of unfolded and partially folded proteins.

@nl

type

label

Equilibrium NMR studies of unfolded and partially folded proteins.

@en

Equilibrium NMR studies of unfolded and partially folded proteins.

@nl

prefLabel

Equilibrium NMR studies of unfolded and partially folded proteins.

@en

Equilibrium NMR studies of unfolded and partially folded proteins.

@nl

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Nature structural biology

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Equilibrium NMR studies of unfolded and partially folded proteins.

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P2860

Solution Structure of the KIX Domain of CBP Bound to the Transactivation Domain of CREB: A Model for Activator:Coactivator Interactions

NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.

Characterization of the backbone dynamics of folded and denatured states of an SH3 domain.

Triple-resonance NOESY-based experiments with improved spectral resolution: applications to structural characterization of unfolded, partially folded and folded proteins.

Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study.

Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin.

Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin.

Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy.

Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding.

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499-503

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10.1038/739

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5 Suppl

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1998-07-01T00:00:00Z

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13620072

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9665178

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protein folding