Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement

G. Marius Clore, Chun Tang, Junji Iwahara

Research output: Contribution to journalArticle

151 Citations (Scopus)

Abstract

Recent advances in the use of paramagnetic relaxation enhancement (PRE) in structure refinement and in the analysis of transient dynamic processes involved in macromolecular complex formation are presented. In the slow exchange regime, we show, using the SRY/DNA complex as an example, that the PRE provides a powerful tool that can lead to significant increases in the reliability and accuracy of NMR structure determinations. Refinement necessitates the use of an ensemble representation of the paramagnetic center and a model-free extension of the Solomon-Bloembergen equations. In the fast exchange regime, the PRE provides insight into dynamic processes and the existence of transient, low population intermediate species. The PRE allows one to characterize dynamic nonspecific binding of a protein to DNA; to directly demonstrate that the search process whereby a transcription factor locates its specific DNA target site involves both intramolecular (sliding) and intermolecular (hopping and intersegment transfer) translocation; and to detect and visualize the distribution of an ensemble of transient encounter complexes in protein-protein association.

Original languageEnglish (US)
Pages (from-to)603-616
Number of pages14
JournalCurrent Opinion in Structural Biology
Volume17
Issue number5
DOIs
StatePublished - Oct 2007
Externally publishedYes

Fingerprint

DNA
Macromolecular Substances
Carrier Proteins
Proteins
Transcription Factors
Population

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement. / Clore, G. Marius; Tang, Chun; Iwahara, Junji.

In: Current Opinion in Structural Biology, Vol. 17, No. 5, 10.2007, p. 603-616.

Research output: Contribution to journalArticle

@article{248e60dab557492fbf5106989e47010d,
title = "Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement",
abstract = "Recent advances in the use of paramagnetic relaxation enhancement (PRE) in structure refinement and in the analysis of transient dynamic processes involved in macromolecular complex formation are presented. In the slow exchange regime, we show, using the SRY/DNA complex as an example, that the PRE provides a powerful tool that can lead to significant increases in the reliability and accuracy of NMR structure determinations. Refinement necessitates the use of an ensemble representation of the paramagnetic center and a model-free extension of the Solomon-Bloembergen equations. In the fast exchange regime, the PRE provides insight into dynamic processes and the existence of transient, low population intermediate species. The PRE allows one to characterize dynamic nonspecific binding of a protein to DNA; to directly demonstrate that the search process whereby a transcription factor locates its specific DNA target site involves both intramolecular (sliding) and intermolecular (hopping and intersegment transfer) translocation; and to detect and visualize the distribution of an ensemble of transient encounter complexes in protein-protein association.",
author = "Clore, {G. Marius} and Chun Tang and Junji Iwahara",
year = "2007",
month = "10",
doi = "10.1016/j.sbi.2007.08.013",
language = "English (US)",
volume = "17",
pages = "603--616",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier Limited",
number = "5",

}

TY - JOUR

T1 - Elucidating transient macromolecular interactions using paramagnetic relaxation enhancement

AU - Clore, G. Marius

AU - Tang, Chun

AU - Iwahara, Junji

PY - 2007/10

Y1 - 2007/10

N2 - Recent advances in the use of paramagnetic relaxation enhancement (PRE) in structure refinement and in the analysis of transient dynamic processes involved in macromolecular complex formation are presented. In the slow exchange regime, we show, using the SRY/DNA complex as an example, that the PRE provides a powerful tool that can lead to significant increases in the reliability and accuracy of NMR structure determinations. Refinement necessitates the use of an ensemble representation of the paramagnetic center and a model-free extension of the Solomon-Bloembergen equations. In the fast exchange regime, the PRE provides insight into dynamic processes and the existence of transient, low population intermediate species. The PRE allows one to characterize dynamic nonspecific binding of a protein to DNA; to directly demonstrate that the search process whereby a transcription factor locates its specific DNA target site involves both intramolecular (sliding) and intermolecular (hopping and intersegment transfer) translocation; and to detect and visualize the distribution of an ensemble of transient encounter complexes in protein-protein association.

AB - Recent advances in the use of paramagnetic relaxation enhancement (PRE) in structure refinement and in the analysis of transient dynamic processes involved in macromolecular complex formation are presented. In the slow exchange regime, we show, using the SRY/DNA complex as an example, that the PRE provides a powerful tool that can lead to significant increases in the reliability and accuracy of NMR structure determinations. Refinement necessitates the use of an ensemble representation of the paramagnetic center and a model-free extension of the Solomon-Bloembergen equations. In the fast exchange regime, the PRE provides insight into dynamic processes and the existence of transient, low population intermediate species. The PRE allows one to characterize dynamic nonspecific binding of a protein to DNA; to directly demonstrate that the search process whereby a transcription factor locates its specific DNA target site involves both intramolecular (sliding) and intermolecular (hopping and intersegment transfer) translocation; and to detect and visualize the distribution of an ensemble of transient encounter complexes in protein-protein association.

UR - http://www.scopus.com/inward/record.url?scp=35548943472&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=35548943472&partnerID=8YFLogxK

U2 - 10.1016/j.sbi.2007.08.013

DO - 10.1016/j.sbi.2007.08.013

M3 - Article

VL - 17

SP - 603

EP - 616

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

IS - 5

ER -