Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering. - Wikidata - wikimedia - TriplyDB

Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.

Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.

http://www.wikidata.org/entity/Q42845790

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Conversion of alpha-lactalbumin to a protein inducing apoptosis alpha-Lactalbumin: structure and function Natively unfolded proteins: a point where biology waits for physics The 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 data Folding-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 form Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy Is 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 proteolysis Carbonic 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.

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P2860

Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.

http://www.wikidata.org/entity/Q42845790

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P2860

Refined structure of baboon alpha-lactalbumin at 1.7 A resolution. Comparison with C-type lysozyme

Residual structure in a staphylococcal nuclease fragment. Is it a molten globule and is its unfolding a first-order phase transition?

Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants.

NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease.

The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

Molten globule of cytochrome c studied by small angle X-ray scattering.

Truncated staphylococcal nuclease is compact but disordered.

Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.

Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway.

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