Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction
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| 024 | 7 | 0 | |a 10.1515/BC.2004.119 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2004.119 | ||
| 100 | 1 | |a Steinhoff |D Heinz-Jürgen |u 1. Fachbereich Physik, Universität Osnabrück, D-49069 Osnabrück, Germany | |
| 245 | 1 | 0 | |a Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction |h [Elektronische Daten] |c [Heinz-Jürgen Steinhoff] |
| 520 | 3 | |a Recent developments including pulse and multi-frequency techniques make the combination of site-directed spin labeling and electron paramagnetic resonance (EPR) spectroscopy an attractive approach for the study of protein-protein or protein-oligonucleotide interaction. Analysis of the spin label side chain mobility, its solvent accessibility, the polarity of the spin label micro-environment and distances between spin label side chains allow the modeling of protein domains or protein-protein 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 intra-molecular 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. | |
| 540 | |a © Walter de Gruyter | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 690 | 7 | |a bacteriorhodopsin |2 nationallicence | |
| 690 | 7 | |a inter-spin distance |2 nationallicence | |
| 690 | 7 | |a proline permease |2 nationallicence | |
| 690 | 7 | |a pulse EPR |2 nationallicence | |
| 690 | 7 | |a sensory rhodopsin |2 nationallicence | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 385/10(2004-10-01), 913-920 |x 1431-6730 |q 385:10<913 |1 2004 |2 385 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2004.119 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2004.119 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 100 |E 1- |a Steinhoff |D Heinz-Jürgen |u 1. Fachbereich Physik, Universität Osnabrück, D-49069 Osnabrück, Germany | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 385/10(2004-10-01), 913-920 |x 1431-6730 |q 385:10<913 |1 2004 |2 385 |o bchm | ||
| 900 | 7 | |b CC0 |u http://creativecommons.org/publicdomain/zero/1.0 |2 nationallicence | |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-gruyter | ||