Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.
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Conversion of alpha-lactalbumin to a protein inducing apoptosisStructural insights into the stability perturbations induced by N-terminal variation in human and goat α-lactalbuminMolecular characterization of alpha-lactalbumin folding variants that induce apoptosis in tumor cellsalpha-Lactalbumin: structure and functionA model of dynamic side-chain--side-chain interactions in the alpha-lactalbumin molten globuleCharacterization of the molten globule state of retinol-binding protein using a molecular dynamics simulation approach.Tracking lysozyme unfolding during salt-induced precipitation with hydrogen exchange and mass spectrometry.NMR elucidation of early folding hierarchy in HIV-1 protease.Capturing molten globule state of α-lactalbumin through constant pH molecular dynamics simulations.HAMLET: functional properties and therapeutic potential.Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques.Folding-unfolding of goat alpha-lactalbumin studied by stopped-flow circular dichroism and molecular dynamics simulations.Effects of organic solvents on protein structures: observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide.Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements.The hydrogen exchange core and protein folding.Studies of biomolecular conformations and conformational dynamics by mass spectrometry.Can misfolded proteins be beneficial? The HAMLET case.The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozymeCan allosteric regulation be predicted from structure?The structural distribution of cooperative interactions in proteins: analysis of the native state ensembleHexafluoroacetone hydrate as a structure modifier in proteins: characterization of a molten globule state of hen egg-white lysozyme.Limited proteolysis of bovine alpha-lactalbumin: isolation and characterization of protein domains.Hydrophobic photolabeling as a new method for structural characterization of molten globule and related protein folding intermediates.Native-state hydrogen-exchange studies of a fragment complex can provide structural information about the isolated fragments.Comparison of protein fragments identified by limited proteolysis and by computational cutting of proteins.Hydrophobic sequence minimization of the alpha-lactalbumin molten globule.Molecular mechanisms of the cytotoxicity of human α-lactalbumin made lethal to tumor cells (HAMLET) and other protein-oleic acid complexes.Global and local indices for characterizing biomolecular flexibility and rigidity.Sequential four-state folding/unfolding of goat α-lactalbumin and its N-terminal variants.The human alpha-lactalbumin molten globule: comparison of structural preferences at pH 2 and pH 7.Pressure-induced unfolding of the molten globule of all-Ala alpha-lactalbumin.Probing the urea dependence of residual structure in denatured human alpha-lactalbumin.Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state.Subdomain interactions as a determinant in the folding and stability of T4 lysozyme.Transition state in the folding of alpha-lactalbumin probed by the 6-120 disulfide bondBiophysical characterization of a beta-peptide bundle: comparison to natural proteinsStructural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR.A comparative study of the alpha-subdomains of bovine and human alpha-lactalbumin reveals key differences that correlate with molten globule stability.
P2860
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P2860
Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.
description
1995 nî lūn-bûn
@nan
1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Different subdomains are most ...... es of human alpha-lactalbumin.
@ast
Different subdomains are most ...... es of human alpha-lactalbumin.
@en
Different subdomains are most ...... es of human alpha-lactalbumin.
@nl
type
label
Different subdomains are most ...... es of human alpha-lactalbumin.
@ast
Different subdomains are most ...... es of human alpha-lactalbumin.
@en
Different subdomains are most ...... es of human alpha-lactalbumin.
@nl
prefLabel
Different subdomains are most ...... es of human alpha-lactalbumin.
@ast
Different subdomains are most ...... es of human alpha-lactalbumin.
@en
Different subdomains are most ...... es of human alpha-lactalbumin.
@nl
P2093
P356
P1476
Different subdomains are most ...... es of human alpha-lactalbumin.
@en
P2093
P304
P356
10.1006/JMBI.1995.0579
P407
P50
P577
1995-11-01T00:00:00Z