about
Biophysical characterization of α-synuclein and its controversial structureProline isomerization in the C-terminal region of HSP27.Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe-S cluster biogenesis.The specialized Hsp70 (HscA) interdomain linker binds to its nucleotide-binding domain and stimulates ATP hydrolysis in both cis and trans configurations.Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes.Automatic Assignment of Methyl-NMR Spectra of Supramolecular Machines Using Graph Theory.Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy.Propensity for cis-Proline Formation in Unfolded Proteins.Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.Disorder in the courtLocal unfolding of the HSP27 monomer regulates chaperone activityHspB1 phosphorylation regulates its intramolecular dynamics and mechanosensitive molecular chaperone interaction with filamin CMonitoring 15N Chemical Shifts During Protein Folding by Pressure-Jump NMRAutomatic structure-based NMR methyl resonance assignment in large proteinsUnveiling invisible protein states with NMR spectroscopy
P50
Q26828504-4DBF9CD9-0E5B-44C9-B089-0E92E517CBCBQ33779914-6F8BCD95-9EA2-4AA1-B718-2277F0D45FC4Q34074450-FAD538AE-AA17-40D8-88CB-4C8AE0B97BC1Q34579866-D97B2E06-1038-4492-904C-D4734BEA491AQ35327865-B67CE68B-478F-49D7-8374-6906FE031A8BQ37079732-E06ED648-6F68-470C-8680-A82EDFEDA578Q38686737-CF507E9E-11DA-415A-B592-E6499835A497Q42354487-EF74E4B1-8400-48F7-95AA-E9507147DE8BQ47610807-D7211F1C-B2F9-49F1-8B80-48045B43532EQ55164334-25BCBB28-E340-4D19-8040-94D676573B75Q59099084-3EA52FF5-DAA1-442A-949A-5A3DEB85DFBEQ64058050-234B26D5-5585-4201-8624-CA893F2C7A10Q64277366-50D00206-21B0-46BB-81AB-DABDE75516BBQ89164112-910DAB6A-35CD-44D2-8E2A-3914AC4A918EQ90998983-A10C3FAC-F29F-43DC-A4D2-EABC3F369808Q91960679-A744C9EF-9BAE-4C3B-B049-37E966FE6FE7
P50
description
investigador
@es
researcher
@en
name
T Reid Alderson
@en
type
label
T Reid Alderson
@en
prefLabel
T Reid Alderson
@en
P21
P31
P496
0000-0001-5163-2276