Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry.
about
The role of the central flexible region on the aggregation and conformational properties of human ataxin-3Mass spectrometry-based methods to study protein architecture and dynamicsChanges in protein structure monitored by use of gas-phase hydrogen/deuterium exchangeCompaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain.Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Top-down study of β2-microglobulin deamidationOrder propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1beta(2)-microglobulin: from physiology to amyloidosis.Advances in ion mobility spectrometry-mass spectrometry reveal key insights into amyloid assembly.Structure and dynamics of oligomeric intermediates in β2-microglobulin self-assembly.Ligand binding to distinct states diverts aggregation of an amyloid-forming protein.Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry.Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry.Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling.DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded formAn improved rapid mixing device for time-resolved electrospray mass spectrometry measurements.Ion Mobility Spectrometry-Mass Spectrometry of Intrinsically Unfolded Proteins: Trying to Put Order into Disorder.HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein beta(2)-microglobulin upon release from the MHC-1.Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein.Insights into the mechanism of protein electrospray ionization from salt adduction measurements.Addressing a Common Misconception: Ammonium Acetate as Neutral pH "Buffer" for Native Electrospray Mass Spectrometry.Deciphering drift time measurements from travelling wave ion mobility spectrometry-mass spectrometry studies.Protein-protein binding affinities in solution determined by electrospray mass spectrometry.Electrospray ionization-mass spectrometry conformational analysis of isolated domains of an intrinsically disordered protein.Characterization of β2-microglobulin conformational intermediates associated to different fibrillation conditions
P2860
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P2860
Co-populated conformational ensembles of beta2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Co-populated conformational en ...... ionization mass spectrometry.
@en
Co-populated conformational en ...... ionization mass spectrometry.
@en-gb
Co-populated conformational en ...... ionization mass spectrometry.
@nl
type
label
Co-populated conformational en ...... ionization mass spectrometry.
@en
Co-populated conformational en ...... ionization mass spectrometry.
@en-gb
Co-populated conformational en ...... ionization mass spectrometry.
@nl
prefLabel
Co-populated conformational en ...... ionization mass spectrometry.
@en
Co-populated conformational en ...... ionization mass spectrometry.
@en-gb
Co-populated conformational en ...... ionization mass spectrometry.
@nl
P2860
P356
P1476
Co-populated conformational en ...... ionization mass spectrometry.
@en
P2093
Antoni J H Borysik
P2860
P304
27069-27077
P356
10.1074/JBC.M401472200
P407
P577
2004-04-20T00:00:00Z