Principal component analysis of the pH-dependent conformational transitions of bovine beta-lactoglobulin monitored by heteronuclear NMR
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Binding Isotherms and Time Courses Readily from Magnetic ResonanceStructure and stability of Gyuba, a β-lactoglobulin chimeraLigand binding and self-association cooperativity of β-lactoglobulinConformational Dynamics and Binding Free Energies of Inhibitors of BACE-1: From the Perspective of Protonation EquilibriaEngineered β-Lactoglobulin Produced in E. coli: Purification, Biophysical and Structural CharacterisationProtein dielectric constants determined from NMR chemical shift perturbationsBovine beta-lactoglobulin acts as an acid-resistant drug carrier by exploiting its diverse binding regions.Remeasuring HEWL pK(a) values by NMR spectroscopy: methods, analysis, accuracy, and implications for theoretical pK(a) calculations.Principal component analysis of chemical shift perturbation data of a multiple-ligand-binding system for elucidation of respective binding mechanism.Fast mapping of global protein folding states by multivariate NMR: a GPS for proteins.Tracking Equilibrium and Nonequilibrium Shifts in Data with TREND.Insight into the glycation of milk proteins: an ESI- and MALDI-MS perspective (review).NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.Mapping allostery through the covariance analysis of NMR chemical shiftsNetwork of long-range concerted chemical shift displacements upon ligand binding to human angiogenin.Protein-RNA specificity by high-throughput principal component analysis of NMR spectraQuantitative analysis of multisite protein-ligand interactions by NMR: binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP.Protein-Inhibitor Interaction Studies Using NMRCracking the allosteric code of NMR chemical shiftsGlycan Activation of a Sheddase: Electrostatic Recognition between Heparin and proMMP-7.Visualizing the principal component of ¹H, ¹⁵N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.Applications of NMR and computational methodologies to study protein dynamics.Network representation of protein interactions: Theory of graph description and analysis.Multiple Ligand-Bound States of a Phosphohexomutase Revealed by Principal Component Analysis of NMR Peak Shifts.Bovine β-lactoglobulin is dimeric under imitative physiological conditions: dissociation equilibrium and rate constants over the pH range of 2.5-7.5.The Mechanism of HdeA Unfolding and Chaperone Activation.
P2860
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P2860
Principal component analysis of the pH-dependent conformational transitions of bovine beta-lactoglobulin monitored by heteronuclear NMR
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2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
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2007年论文
@zh-cn
name
Principal component analysis o ...... monitored by heteronuclear NMR
@ast
Principal component analysis o ...... monitored by heteronuclear NMR
@en
type
label
Principal component analysis o ...... monitored by heteronuclear NMR
@ast
Principal component analysis o ...... monitored by heteronuclear NMR
@en
prefLabel
Principal component analysis o ...... monitored by heteronuclear NMR
@ast
Principal component analysis o ...... monitored by heteronuclear NMR
@en
P2860
P356
P1476
Principal component analysis o ...... monitored by heteronuclear NMR
@en
P2093
Kazumasa Sakurai
P2860
P304
15346-15351
P356
10.1073/PNAS.0702112104
P407
P577
2007-09-18T00:00:00Z