Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.
about
Conversion of alpha-lactalbumin to a protein inducing apoptosisalpha-Lactalbumin: structure and functionNatively unfolded proteins: a point where biology waits for physicsThe impact of protein disulfide bonds on the amyloid fibril morphology.Understanding protein non-folding.Capturing molten globule state of α-lactalbumin through constant pH molecular dynamics simulations.Molecular dynamics model structures for the molten globule state of alpha-lactalbumin: aromatic residue clusters I and II.Design of single-layer beta-sheets without a hydrophobic core.Protein unfolding transitions in an intrinsically unstable annexin domain: molecular dynamics simulation and comparison with nuclear magnetic resonance dataFolding-unfolding of goat alpha-lactalbumin studied by stopped-flow circular dichroism and molecular dynamics simulations.The methanol-induced transition and the expanded helical conformation in hen lysozyme.The compact and expanded denatured conformations of apomyoglobin in the methanol-water solvent.Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein.Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.Effect of a concentrated "inert" macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: a statistical-thermodynamic model.Distribution, transition and thermodynamic stability of protein conformations in the denaturant-induced unfolding of proteins.Macromolecular crowding induces holo α-lactalbumin aggregation by converting to its apo formProtein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopyIs there or isn't there? The case for (and against) residual structure in chemically denatured proteins.Design and characterization of the anion-sensitive coiled-coil peptide.Limited proteolysis of bovine alpha-lactalbumin: isolation and characterization of protein domains.The acid-induced folded state of Sac7d is the native state.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.Partly folded states of members of the lysozyme/lactalbumin superfamily: a comparative study by circular dichroism spectroscopy and limited proteolysisCarbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.Is supramolecular filament chirality the underlying cause of major morphology differences in amyloid fibrils?Molecular dynamics of thermoenzymes at high temperature and pressure: a review.Non-sequence-specific interactions can account for the compaction of proteins unfolded under "native" conditions.Investigation of the Polymeric Properties of α-Synuclein and Comparison with NMR Experiments: A Replica Exchange Molecular Dynamics Study.Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor.Pressure-induced unfolding of the molten globule of all-Ala alpha-lactalbumin.How general is the nucleation-condensation mechanism?The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: fractionation of conformational isomers of alpha-lactalbumin.Stepwise proteolytic removal of the beta subdomain in alpha-lactalbumin. The protein remains folded and can form the molten globule in acid solution.Role of C-terminal region of Staphylococcal nuclease for foldability, stability, and activity.Molten globule of bovine alpha-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis.Small-angle X-ray scattering of BAMLET at pH 12: a complex of α-lactalbumin and oleic acid.Design and Synthesis of a Water-Stable Anionic Uranium-Based Metal-Organic Framework (MOF) with Ultra Large Pores.Role of Charge and Hydrophobicity in Liprotide Formation: A Molecular Dynamics Study with Experimental Constraints.Under-folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis.
P2860
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P2860
Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Structural characterization of ...... by solution X-ray scattering.
@en
Structural characterization of ...... by solution X-ray scattering.
@nl
type
label
Structural characterization of ...... by solution X-ray scattering.
@en
Structural characterization of ...... by solution X-ray scattering.
@nl
prefLabel
Structural characterization of ...... by solution X-ray scattering.
@en
Structural characterization of ...... by solution X-ray scattering.
@nl
P2093
P2860
P356
P1433
P1476
Structural characterization of ...... by solution X-ray scattering.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560060219
P577
1997-02-01T00:00:00Z