Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
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Analytical Aspects of Hydrogen Exchange Mass SpectrometryMechanisms and uses of hydrogen exchange.Fast hydrogen exchange affects ¹⁵N relaxation measurements in intrinsically disordered proteins.A facile route to tailoring peptide-stabilized gold nanoparticles using glutathione as a synthon.NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126.Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol.Effects of organic solvents on protein structures: observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide.Chemoselective 15N tag for sensitive and high-resolution nuclear magnetic resonance profiling of the carboxyl-containing metabolome.Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experimentsProbing solvent accessibility of amyloid fibrils by solution NMR spectroscopyGlycerol-enhanced detection of a preferential structure latent in unstructured 1SS-variants of lysozyme.Probing the conformation of a prion protein fibril with hydrogen exchange.Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR.The transcriptional repressor domain of Gli3 is intrinsically disorderedAmyloid-like fibrils from a domain-swapping protein feature a parallel, in-register conformation without native-like interactions.Characterization of the N-terminal tail domain of histone H3 in condensed nucleosome arrays by hydrogen exchange and NMR.Early stages of amyloid fibril formation studied by liquid-state NMR: the peptide hormone glucagon.The use of spin desalting columns in DMSO-quenched H/D-exchange NMR experiments.Ubiquitin utilizes an acidic surface patch to alter chromatin structure.Spectroscopic elucidation of the inhibitory mechanism of Cys2His2 zinc finger transcription factors by cobalt(III) Schiff base complexes.Folding of apomyoglobin: Analysis of transient intermediate structure during refolding using quick hydrogen deuterium exchange and NMR.Identification of a novel high affinity copper binding site in the APP(145-155) fragment of amyloid precursor protein.A structural study of the self-assembly of a palmitoyl peptide amphiphile.How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.A 31-residue peptide induces aggregation of tau's microtubule-binding region in cells.
P2860
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P2860
Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Rapid amide proton exchange ra ...... ching and two-dimensional NMR.
@ast
Rapid amide proton exchange ra ...... ching and two-dimensional NMR.
@en
type
label
Rapid amide proton exchange ra ...... ching and two-dimensional NMR.
@ast
Rapid amide proton exchange ra ...... ching and two-dimensional NMR.
@en
prefLabel
Rapid amide proton exchange ra ...... ching and two-dimensional NMR.
@ast
Rapid amide proton exchange ra ...... ching and two-dimensional NMR.
@en
P2860
P356
P1433
P1476
Rapid amide proton exchange ra ...... nching and two-dimensional NMR
@en
P2093
P2860
P304
P356
10.1002/PRO.5560040420
P577
1995-04-01T00:00:00Z