Real-time monitoring of protein complexes reveals their quaternary organization and dynamics.
about
Detection of crosslinks within and between proteins by LC-MALDI-TOFTOF and the software FINDX to reduce the MSMS-data to acquire for validationMass spectrometry quantifies protein interactions--from molecular chaperones to membrane porins.Quaternary dynamics and plasticity underlie small heat shock protein chaperone functionMechanistic differences between two conserved classes of small heat shock proteins found in the plant cytosol.Evidence for a quasi-equilibrium distribution of states for bradykinin [M + 3H]3+ ions in the gas phaseProbing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry.Mass spectrometry: come of age for structural and dynamical biology.Revealing ligand binding sites and quantifying subunit variants of noncovalent protein complexes in a single native top-down FTICR MS experimentElectrothermal supercharging of proteins in native electrospray ionization.The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated.New supercharging reagents produce highly charged protein ions in native mass spectrometry.Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones.Mass spectrometry-based monitoring of millisecond protein-ligand binding dynamics using an automated microfluidic platformReceiver domains control the active-state stoichiometry of Aquifex aeolicus sigma54 activator NtrC4, as revealed by electrospray ionization mass spectrometry.The ferritin superfamily: Supramolecular templates for materials synthesis.Protein-nucleic acid complexes and the role of mass spectrometry in their structure determination.Capturing protein structural kinetics by mass spectrometry.Two decades of studying non-covalent biomolecular assemblies by means of electrospray ionization mass spectrometry.Escherichia coli single-stranded DNA-binding protein: nanoESI-MS studies of salt-modulated subunit exchange and DNA binding transactions.The growing world of small heat shock proteins: from structure to functions.How far can we go with structural mass spectrometry of protein complexes?C-terminal interactions mediate the quaternary dynamics of αB-crystallin.Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles.Electrothermal supercharging of proteins in native MS: effects of protein isoelectric point, buffer, and nanoESI-emitter tip size.An improved rapid mixing device for time-resolved electrospray mass spectrometry measurements.Mass, mobility and MSn measurements of single ions using charge detection mass spectrometry.Novel sheathless CE-MS interface as an original and powerful infusion platform for nanoESI study: from intact proteins to high molecular mass noncovalent complexes.Hsp70 displaces small heat shock proteins from aggregates to initiate protein refolding.The unusual mycobacterial chaperonins: evidence for in vivo oligomerization and specialization of function.Monitoring the dynamics of monomer exchange using electrospray mass spectrometry: the case of the dimeric glucosamine-6-phosphate synthase.
P2860
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P2860
Real-time monitoring of protein complexes reveals their quaternary organization and dynamics.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Real-time monitoring of protei ...... ary organization and dynamics.
@en
type
label
Real-time monitoring of protei ...... ary organization and dynamics.
@en
prefLabel
Real-time monitoring of protei ...... ary organization and dynamics.
@en
P2093
P50
P1476
Real-time monitoring of protei ...... nary organization and dynamics
@en
P2093
Alexander J Painter
Eman Basha
Nomalie Jaya
P304
P356
10.1016/J.CHEMBIOL.2008.01.009
P577
2008-03-01T00:00:00Z