Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractNMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH    Next Abstract"Evaluation of the physicochemical, metabolomic, and sensory characteristics of Chikso and Hanwoo beef during wet aging" »

J Magn Reson


Title:Effective rotational correlation times of proteins from NMR relaxation interference
Author(s):Lee D; Hilty C; Wider G; Wuthrich K;
Address:"Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule (ETH), CH-8093 Zurich, Switzerland"
Journal Title:J Magn Reson
Year:2006
Volume:20050926
Issue:1
Page Number:72 - 76
DOI: 10.1016/j.jmr.2005.08.014
ISSN/ISBN:1090-7807 (Print) 1090-7807 (Linking)
Abstract:"Knowledge of the effective rotational correlation times, tauc, for the modulation of anisotropic spin-spin interactions in macromolecules subject to Brownian motion in solution is of key interest for the practice of NMR spectroscopy in structural biology. The value of tauc enables an estimate of the NMR spin relaxation rates, and indicates possible aggregation of the macromolecular species. This paper reports a novel NMR pulse scheme, [15N,1H]-TRACT, which is based on transverse relaxation-optimized spectroscopy and permits to determine tauc for 15N-1H bonds without interference from dipole-dipole coupling of the amide proton with remote protons. [15N,1H]-TRACT is highly efficient since only a series of one-dimensional NMR spectra need to be recorded. Its use is suggested for a quick estimate of the rotational correlation time, to monitor sample quality and to determine optimal parameters for complex multidimensional NMR experiments. Practical applications are illustrated with the 110 kDa 7,8-dihydroneopterin aldolase from Staphylococcus aureus, the uniformly 15N-labeled Escherichia coli outer membrane protein X (OmpX) in 60 kDa mixed OmpX/DHPC micelles with approximately 90 molecules of unlabeled 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC), and the 16 kDa pheromone-binding protein from Bombyx mori, which cover a wide range of correlation times"
Keywords:"Aldehyde-Lyases/*chemistry Anisotropy Escherichia coli Proteins/*chemistry Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular/*methods Staphylococcus aureus/enzymology;"
Notes:"MedlineLee, Donghan Hilty, Christian Wider, Gerhard Wuthrich, Kurt eng Research Support, Non-U.S. Gov't 2005/09/29 J Magn Reson. 2006 Jan; 178(1):72-6. doi: 10.1016/j.jmr.2005.08.014. Epub 2005 Sep 26"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 22-11-2024