Crystal structures of apo- and holo-bovine alpha-lactalbumin at 2. 2-A resolution reveal an effect of calcium on inter-lobe interactions
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A united residue force-field for calcium-protein interactions.Predictive approach for protein aggregation: Correlation of protein surface characteristics and conformational flexibility to protein aggregation propensity.Integration of Diverse Research Methods to Analyze and Engineer Ca-Binding Proteins: From Prediction to ProductionImproving structure-based function prediction using molecular dynamics.Low resolution solution structure of HAMLET and the importance of its alpha-domains in tumoricidal activity.Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.Influence of pH on the structure and oleic acid binding ability of bovine α-lactalbumin.Macromolecular crowding induces holo α-lactalbumin aggregation by converting to its apo formThe cytotoxicity of BAMLET complexes is due to oleic acid and independent of the α-lactalbumin component.Toward a molecular understanding of protein solubility: increased negative surface charge correlates with increased solubilityPatterns of protein protein interactions in salt solutions and implications for protein crystallization.Lipids as cofactors in protein folding: stereo-specific lipid-protein interactions are required to form HAMLET (human alpha-lactalbumin made lethal to tumor cells).Probing protein conformation with a minimal photochemical reagent.Partly folded states of members of the lysozyme/lactalbumin superfamily: a comparative study by circular dichroism spectroscopy and limited proteolysisEffects of metal ion adduction on the gas-phase conformations of protein ions.Protein-dependent Membrane Interaction of A Partially Disordered Protein Complex with Oleic Acid: Implications for Cancer Lipidomics.Conformation and orientation of a protein folding intermediate trapped by adsorption.Bioactivity of α-lactalbumin related to its interaction with fatty acids: a review.Structure of allergens and structure based epitope predictions.Impact of the environmental conditions and substrate pre-treatment on whey protein hydrolysis: A review.The effect of nanoscale surface curvature on the oligomerization of surface-bound proteinsElectrostatic interactions play an essential role in the binding of oleic acid with α-lactalbumin in the HAMLET-like complex: a study using charge-specific chemical modifications.Structural basis for difference in heat capacity increments for Ca(2+) binding to two alpha-lactalbumins.pH-dependence of single-protein adsorption and diffusion at a liquid chromatographic interface.Using THz Spectroscopy, Evolutionary Network Analysis Methods, and MD Simulation to Map the Evolution of Allosteric Communication Pathways in c-Type Lysozymes.Alpha-lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human alpha-lactalbumin made lethal to tumor cells)A combined tryptic peptide and winged peptide internal standard approach for the determination of α-lactalbumin in dairy products by ultra high performance liquid chromatography with tandem mass spectrometry.Predicting Ca2+ -binding sites using refined carbon clusters.Cofactor effects on the protein folding reaction: acceleration of alpha-lactalbumin refolding by metal ions.Stability of HAMLET--a kinetically trapped alpha-lactalbumin oleic acid complex.Comparative study on heat stability of camel and bovine apo and holo 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.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.Role of Charge and Hydrophobicity in Liprotide Formation: A Molecular Dynamics Study with Experimental Constraints.Photophysics, photochemistry and energetics of UV light induced disulphide bridge disruption in apo-α-lactalbumin.L-arginine induces protein aggregation and transformation of supramolecular structures of the aggregates.Interleukin-11 binds specific EF-hand proteins via their conserved structural motifs.How to improve nature: study of the electrostatic properties of the surface of alpha-lactalbumin.Orientation of polar molecules near charged protein interfaces.
P2860
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P2860
Crystal structures of apo- and holo-bovine alpha-lactalbumin at 2. 2-A resolution reveal an effect of calcium on inter-lobe interactions
description
2000 nî lūn-bûn
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2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Crystal structures of apo- and ...... ium on inter-lobe interactions
@ast
Crystal structures of apo- and ...... ium on inter-lobe interactions
@en
Crystal structures of apo- and ...... ium on inter-lobe interactions
@nl
type
label
Crystal structures of apo- and ...... ium on inter-lobe interactions
@ast
Crystal structures of apo- and ...... ium on inter-lobe interactions
@en
Crystal structures of apo- and ...... ium on inter-lobe interactions
@nl
prefLabel
Crystal structures of apo- and ...... ium on inter-lobe interactions
@ast
Crystal structures of apo- and ...... ium on inter-lobe interactions
@en
Crystal structures of apo- and ...... ium on inter-lobe interactions
@nl
P2860
P3181
P356
P1476
Crystal structures of apo- and ...... ium on inter-lobe interactions
@en
P2093
P2860
P304
P3181
P356
10.1074/JBC.M004752200
P407
P577
2000-11-24T00:00:00Z