Structure and energetics of the hydrogen-bonded backbone in protein folding.
about
Residual structure in unfolded proteinsMacromolecule-assisted de novo protein foldingElucidating the exact role of engineered CRABPII residues for the formation of a retinal protonated Schiff baseThe use of trimethylamineN-oxide as a primary precipitating agent and related methylamine osmolytes as cryoprotective agents for macromolecular crystallographySingle amino acid exchange in bacteriophage HK620 tailspike protein results in thousand-fold increase of its oligosaccharide affinityDesign of thermostable rhamnogalacturonan lyase mutants from Bacillus licheniformis by combination of targeted single point mutationsCholesterol oxidase: ultrahigh-resolution crystal structure and multipolar atom model-based analysisConformational transitions of the cross-linking domains of elastin during self-assemblyCosolvent and crowding effects on the polymerization kinetics of actin.Structures, basins, and energies: a deconstruction of the Protein Coil Library.Salts employed in hydrophobic interaction chromatography can change protein structure - insights from protein-ligand interaction thermodynamics, circular dichroism spectroscopy and small angle X-ray scattering.Analysis of repeat-protein folding using nearest-neighbor statistical mechanical modelsHow osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory.Physical-chemical determinants of coil conformations in globular proteins.Protein folding at single-molecule resolution.The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studiesAn analysis of the influence of protein intrinsic dynamical properties on its thermal unfolding behavior.Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Plasticity of hydrogen bond networks regulates mechanochemistry of cell adhesion complexes.Importance of backbone and solvent properties for conformational dynamics in polypeptides.Consistent picture of the reversible thermal unfolding of hen egg-white lysozyme from experiment and molecular dynamicsBackbone additivity in the transfer model of protein solvation.Rescue of glaucoma-causing mutant myocilin thermal stability by chemical chaperones.Net charge per residue modulates conformational ensembles of intrinsically disordered proteinsSolubility and aggregation of Gly(5) in water.From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins.Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm.When does trimethylamine N-oxide fold a polymer chain and urea unfold it?The osmolyte TMAO stabilizes native RNA tertiary structures in the absence of Mg2+: evidence for a large barrier to folding from phosphate dehydration.Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturationRedrawing the Ramachandran plot after inclusion of hydrogen-bonding constraints.Stabilization of the predominant disease-causing aldolase variant (A149P) with zwitterionic osmolytesPeptide conformational preferences in osmolyte solutions: transfer free energies of decaalanine.Minimalistic predictor of protein binding energy: contribution of solvation factor to protein binding.Structural dynamics, intrinsic disorder, and allostery in nuclear receptors as transcription factors.Manifestations of native topology in the denatured state ensemble of Rhodopseudomonas palustris cytochrome c'.A thermodynamic definition of protein domainsSolute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding abilityDenaturation of RNA secondary and tertiary structure by urea: simple unfolded state models and free energy parameters account for measured m-values.
P2860
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P2860
Structure and energetics of the hydrogen-bonded backbone in protein folding.
description
2008 nî lūn-bûn
@nan
2008 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Structure and energetics of the hydrogen-bonded backbone in protein folding.
@ast
Structure and energetics of the hydrogen-bonded backbone in protein folding.
@en
type
label
Structure and energetics of the hydrogen-bonded backbone in protein folding.
@ast
Structure and energetics of the hydrogen-bonded backbone in protein folding.
@en
prefLabel
Structure and energetics of the hydrogen-bonded backbone in protein folding.
@ast
Structure and energetics of the hydrogen-bonded backbone in protein folding.
@en
P1476
Structure and energetics of the hydrogen-bonded backbone in protein folding.
@en
P2093
D Wayne Bolen
George D Rose
P304
P356
10.1146/ANNUREV.BIOCHEM.77.061306.131357
P577
2008-01-01T00:00:00Z