A residue-specific NMR view of the non-cooperative unfolding of a molten globule
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Is the molten globule a third phase of proteins?Cold denaturation of a protein dimer monitored at atomic resolutionA partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited foldingAmyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation.Characterization of the structure and dynamics of a near-native equilibrium intermediate in the unfolding pathway of an all beta-barrel protein.Identification and characterization of an equilibrium intermediate in the unfolding pathway of an all beta-barrel protein.Overview on the use of NMR to examine protein structure.Clustering of low-energy conformations near the native structures of small proteins.Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques.NMR characterization of partially folded and unfolded conformational ensembles of proteins.Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.FlgM gains structure in living cells.Structures and relative free energies of partially folded states of proteinsProtein dynamics governed by interfaces of high polarity and low packing density.An amino acid code for protein foldingThe client protein p53 adopts a molten globule-like state in the presence of Hsp90.The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding.A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin.Mapping of the CD23 binding site on immunoglobulin E (IgE) and allosteric control of the IgE-Fc epsilonRI interactionProbing protein conformation with a minimal photochemical reagent.Comparison of protein fragments identified by limited proteolysis and by computational cutting of proteins.Hydrophobic sequence minimization of the alpha-lactalbumin molten globule.New structural insights into Golgi Reassembly and Stacking Protein (GRASP) in solution.Conformational properties of beta-PrP.Trichloroacetic acid-induced protein precipitation involves the reversible association of a stable partially structured intermediate.Rational design of a conformation-switchable Ca2+- and Tb3+-binding protein without the use of multiple coupled metal-binding sites.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.The cytochrome c fold can be attained from a compact apo state by occupancy of a nascent heme binding site.The unfolding mechanism and the disulfide structures of denatured lysozyme.Effects of a helix substitution on the folding mechanism of bovine alpha-lactalbumin.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.Equilibrium NMR studies of unfolded and partially folded proteins.Secondary structure conversions of Alzheimer's Abeta(1-40) peptide induced by membrane-mimicking detergents.Protein folding intermediates of invasin protein IbeA from Escherichia coli.Kinetic studies of protein folding using NMR spectroscopy.Recovering Invisible Signals by Two-Field NMR Spectroscopy.Molecular dynamics simulations of human alpha-lactalbumin: changes to the structural and dynamical properties of the protein at low pH.Molten globule state of human placental cystatin (HPC) at low pH conditions and the effects of trifluoroethanol (TFE) and methanol.
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A residue-specific NMR view of the non-cooperative unfolding of a molten globule
description
scientific article published on 01 August 1997
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wetenschappelijk artikel
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наукова стаття, опублікована в серпні 1997
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name
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
@en
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
@nl
type
label
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
@en
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
@nl
prefLabel
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
@en
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
@nl
P2093
P2860
P356
P1476
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
@en
P2093
P2860
P304
P356
10.1038/NSB0897-630
P577
1997-08-01T00:00:00Z