Probing dynamic conformations of the high-molecular-weight αB-crystallin heat shock protein ensemble by NMR spectroscopy.
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Mechanisms of amyloid formation revealed by solution NMRFacing and Overcoming Sensitivity Challenges in Biomolecular NMR SpectroscopyQuantification of anti-aggregation activity of chaperones: a test-system based on dithiothreitol-induced aggregation of bovine serum albuminFunctions of crystallins in and out of lens: roles in elongated and post-mitotic cellsCapturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular ModelingMeasuring hydrogen exchange rates in invisible protein excited statesInvestigating the mechanisms of amylolysis of starch granules by solution-state NMR.Proline isomerization in the C-terminal region of HSP27.A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein OligomersOligomers of Heat-Shock Proteins: Structures That Don't Imply Function.Perturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme ActivityEvolution of crystallins for a role in the vertebrate eye lens.One size does not fit all: the oligomeric states of αB crystallin.The growing world of small heat shock proteins: from structure to functions.Intermolecular Interactions and Protein Dynamics by Solid-State NMR Spectroscopy.C-terminal interactions mediate the quaternary dynamics of αB-crystallin.Intermolecular Interactions and Protein Dynamics by Solid-State NMR SpectroscopyAn exact solution for R2,eff in CPMG experiments in the case of two site chemical exchangeFormation kinetics and structural features of Beta-amyloid aggregates by sedimented solute NMR.HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.Novel insights in the disease biology of mutant small heat shock proteins in neuromuscular diseases.The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.An R(1ρ) expression for a spin in chemical exchange between two sites with unequal transverse relaxation rates.SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR.Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. Effect of crowding agents and chaperonesSSNMR of biosilica-entrapped enzymes permits an easy assessment of preservation of native conformation in atomic detailPractical considerations over spectral quality in solid state NMR spectroscopy of soluble proteinsNeue Ansätze zur Empfindlichkeitssteigerung in der biomolekularen NMR-Spektroskopie
P2860
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P2860
Probing dynamic conformations of the high-molecular-weight αB-crystallin heat shock protein ensemble by NMR spectroscopy.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Probing dynamic conformations ...... ensemble by NMR spectroscopy.
@en
Probing dynamic conformations ...... ensemble by NMR spectroscopy.
@nl
type
label
Probing dynamic conformations ...... ensemble by NMR spectroscopy.
@en
Probing dynamic conformations ...... ensemble by NMR spectroscopy.
@nl
prefLabel
Probing dynamic conformations ...... ensemble by NMR spectroscopy.
@en
Probing dynamic conformations ...... ensemble by NMR spectroscopy.
@nl
P2093
P50
P356
P1476
Probing dynamic conformations ...... n ensemble by NMR spectroscopy
@en
P2093
Andrew J Baldwin
Gillian R Hilton
Lewis E Kay
Simon Sharpe
P304
15343-15350
P356
10.1021/JA307874R
P407
P577
2012-09-07T00:00:00Z