Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction

Autor(en): Steinhoff, HJ
Stichwörter: bacteriorhodopsin; Biochemistry & Molecular Biology; CONFORMATIONAL-CHANGES; HELIX-F; HIGH-FIELD EPR; inter-spin distance; INTERSPIN DISTANCES; LACTOSE PERMEASE; MEMBRANE-PROTEIN; NA+/PROLINE TRANSPORTER; proline permease; pulse EPR; sensory rhodopsin; SENSORY RHODOPSIN-II; TET REPRESSOR; TIME-RESOLVED DETECTION
Erscheinungsdatum: 2004
Herausgeber: WALTER DE GRUYTER GMBH
Journal: BIOLOGICAL CHEMISTRY
Volumen: 385
Ausgabe: 10
Startseite: 913
Seitenende: 920
Zusammenfassung: 
Recent developments including pulse and multifrequency techniques make the combination of sitedirected spin labeling and electron paramagnetic resonance (EPR) spectroscopy an attractive approach for the study of protein protein or proteinoligonucleotide interaction. Analysis of the spin label side chain mobility, its solvent accessibility, the polarity of the spin label microenvironment and distances between spin label side chains allow the modeling of protein domains or proteinprotein interaction sites and their conformational changes with a spatial resolution at the level of the backbone fold. Structural changes can be detected with millisecond time resolution. Inter and intramolecular distances are accessible in the range from approximately 0.5 to 8 nm by the combination of continuous wave and pulse EPR methods. Recent applications include the study of transmembrane substrate transport, membrane channel gating, gene regulation and signal transfer.
ISSN: 14316730
DOI: 10.1515/BC.2004.119

Show full item record

Page view(s)

1
Last Week
0
Last month
0
checked on Mar 3, 2024

Google ScholarTM

Check

Altmetric