Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry.
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Chemical structure identification in metabolomics: computational modeling of experimental featuresThe roles of conditional disorder in redox proteinsThe hepatitis B virus preS1 domain hijacks host trafficking proteins by motif mimicryChanges in protein structure monitored by use of gas-phase hydrogen/deuterium exchangeIrreversible thermal denaturation of cytochrome C studied by electrospray mass spectrometry.Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain.Novel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry.Amphitrite: A program for processing travelling wave ion mobility mass spectrometry data.An ion trap-ion mobility-time of flight mass spectrometer with three ion sources for ion/ion reactions.Elongated oligomers in beta2-microglobulin amyloid assembly revealed by ion mobility spectrometry-mass spectrometry.Unraveling the early events of amyloid-β protein (Aβ) aggregation: techniques for the determination of Aβ aggregate size.The N-terminal residues 43 to 60 form the interface for dopamine mediated α-synuclein dimerisation.Simultaneous analysis of enzyme structure and activity by kinetic capillary electrophoresis-MS.Retention of glycopeptides analyzed using hydrophilic interaction chromatography is influenced by charge and carbon chain length of ion-pairing reagent for mobile phase.MolFind: a software package enabling HPLC/MS-based identification of unknown chemical structures.The role of initial oligomers in amyloid fibril formation by human stefin B.Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1Structural characterization of unsaturated phosphatidylcholines using traveling wave ion mobility spectrometry.Ion Mobility-Mass Spectrometry Analysis of Cross-Linked Intact Multiprotein Complexes: Enhanced Gas-Phase Stabilities and Altered Dissociation Pathways.beta(2)-microglobulin: from physiology to amyloidosis.Large-scale production and structural and biophysical characterizations of the human hepatitis B virus polymerase.Ion mobility mass spectrometry of proteins and protein assemblies.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.Unraveling lactococcal phage baseplate assembly by mass spectrometryA novel rapid analysis using mass spectrometry to evaluate downstream refolding of recombinant human insulin-like growth factor-1 (mecasermin).'From past to future' - deciphering the molecular basis of Alzheimer's disease through the pages of the Journal of Neurochemistry.Native Mass Spectrometry: What is in the Name?A tale of a tail: Structural insights into the conformational properties of the polyglutamine protein ataxin-3.Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS.Using ion mobility spectrometry-mass spectrometry to decipher the conformational and assembly characteristics of the hepatitis B capsid protein.Protein destabilisation by ruthenium(II) tris-bipyridine based protein-surface mimeticsFundamentals of traveling wave ion mobility spectrometryDE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded formIon Mobility Spectrometry-Mass Spectrometry of Intrinsically Unfolded Proteins: Trying to Put Order into Disorder.The role of conformational flexibility in β2-microglobulin amyloid fibril formation at neutral pH.Ion mobility spectrometry focusing on speciation analysis of metals/metalloids bound to carbonic anhydrase.Mass spectrometric characterization of protein structures and protein complexes in condensed and gas phase.Comparing equilibrium and kinetic protein unfolding using time-resolved electrospray-coupled ion mobility mass spectrometry.
P2860
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P2860
Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry.
description
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
@zh
2007年论文
@zh-cn
name
Monitoring copopulated conform ...... pectrometry-mass spectrometry.
@en
Monitoring copopulated conform ...... pectrometry-mass spectrometry.
@en-gb
type
label
Monitoring copopulated conform ...... pectrometry-mass spectrometry.
@en
Monitoring copopulated conform ...... pectrometry-mass spectrometry.
@en-gb
prefLabel
Monitoring copopulated conform ...... pectrometry-mass spectrometry.
@en
Monitoring copopulated conform ...... pectrometry-mass spectrometry.
@en-gb
P2860
P50
P1476
Monitoring copopulated conform ...... pectrometry-mass spectrometry.
@en
P2093
Kevin Giles
Robert H Bateman
P2860
P2888
P304
P356
10.1016/J.JASMS.2007.09.017
P577
2007-10-02T00:00:00Z
P5875
P6179
1004867090