about
From snapshot to movie: phi analysis of protein folding transition states taken one step furtherNMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigensBetaCore, a designed water soluble four-stranded antiparallel β-sheet proteinAutoinhibition of ETV6 (TEL) DNA Binding: Appended Helices Sterically Block the ETS DomainSolution Structure of CXCL5 — A Novel Chemokine and Adipokine Implicated in Inflammation and ObesityAmide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchangeStart2Fold: a database of hydrogen/deuterium exchange data on protein folding and stabilityDetecting structural changes in viral capsids by hydrogen exchange and mass spectrometryPartial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel proteinCharacterization of the structure and dynamics of a near-native equilibrium intermediate in the unfolding pathway of an all beta-barrel protein.Identification of rare partially unfolded states in equilibrium with the native conformation in an all beta-barrel protein.Conformation and stability of thiol-modified bovine beta-lactoglobulin.Mapping oxygen accessibility to ribonuclease a using high-resolution NMR relaxation spectroscopyShorter side chains optimize helix-helix packing.Probing protein structure and dynamics by hydrogen exchange-mass spectrometry.Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry.Hydrogen exchange monitored by MALDI-TOF mass spectrometry for rapid characterization of the stability and conformation of proteins.Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?Characterization of intermolecular beta-sheet peptides by mass spectrometry and hydrogen isotope exchange.Cavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozymeHow amide hydrogens exchange in native proteinsClusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stability.Predicting protein folding pathways at the mesoscopic level based on native interactions between secondary structure elements.Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements.Investigating homology between proteins using energetic profilesProtein unfolding: rigidity lost.Deuterium/hydrogen exchange factors measured by solution nuclear magnetic resonance spectroscopy as indicators of the structure and topology of membrane proteinsChanges in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange.Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding.Enhancing the stability and folding rate of a repeat protein through the addition of consensus repeatsA delicate interplay of structure, dynamics, and thermodynamics for function: a high pressure NMR study of outer surface protein A.Adaptive local learning in sampling based motion planning for protein folding.Scope and utility of hydrogen exchange as a tool for mapping landscapesThe folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stabilityEnhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrilsFolding and assembly of large macromolecular complexes monitored by hydrogen-deuterium exchange and mass spectrometry.Dynameomics: large-scale assessment of native protein flexibility.Predicting protein folding cores by empirical potential functions.Proline substitution of dimer interface β-strand residues as a strategy for the design of functional monomeric proteins.
P2860
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P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The hydrogen exchange core and protein folding.
@ast
The hydrogen exchange core and protein folding.
@en
type
label
The hydrogen exchange core and protein folding.
@ast
The hydrogen exchange core and protein folding.
@en
prefLabel
The hydrogen exchange core and protein folding.
@ast
The hydrogen exchange core and protein folding.
@en
P2860
P356
P1433
P1476
The hydrogen exchange core and protein folding
@en
P2093
C Woodward
P2860
P304
P356
10.1110/PS.8.8.1571
P50
P577
1999-08-01T00:00:00Z