Related ArticlesSolution NMR Structure Determination of Polytopic ?-Helical Membrane Proteins: A Guide to Spin Label Paramagnetic Relaxation Enhancement Restraints.
Methods Enzymol. 2015;557:329-348
Authors: Columbus L, Kroncke B
Abstract
Solution nuclear magnetic resonance structures of polytopic ?-helical membrane proteins require additional restraints beyond the traditional Nuclear Overhauser Effect (NOE) restraints. Several methods have been developed and this review focuses on paramagnetic relaxation enhancement (PRE). Important aspects of spin labeling, PRE measurements, structure calculations, and structural quality are discussed.
PMID: 25950972 [PubMed - as supplied by publisher]
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Abstract
The use of paramagnetic constraints in protein NMR is an active area of research because of the benefits of long-range distance measurements (>10Â*Ã?). One of the main issues in successful execution is the incorporation of a paramagnetic metal ion into diamagnetic proteins. The most common metal ion tags are relatively long aliphatic chains attached to the side chain of a...
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11-28-2014 11:37 AM
[NMR paper] Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints.
Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints.
Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints.
J Biomol NMR. 2014 Nov 27;
Authors: Furuita K, Kataoka S, Sugiki T, Hattori Y, Kobayashi N, Ikegami T, Shiozaki K, Fujiwara T, Kojima C
Abstract
NMR structure determination of soluble proteins...
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11-28-2014 11:37 AM
Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints
Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints
Abstract
NMR structure determination of soluble proteins depends in large part on distance restraints derived from NOE. In this study, we examined the impact of paramagnetic relaxation enhancement (PRE)-derived distance restraints on protein structure determination. A high-resolution structure of the loop-rich soluble protein Sin1 could not be determined by conventional NOE-based...
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11-26-2014 10:50 PM
[NMR paper] Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Biochim Biophys Acta. 2013 Jul 2;
Authors: Gautier A
Abstract
The biochemical processes of living cells involve a numerous series of reactions that work with exceptional specificity and efficiency. The tight control of this intricate reaction network stems from the architecture of the proteins that drive the chemical...
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07-09-2013 02:47 PM
Structure determination of ?–helical membrane proteins by solution-state NMR: Emphasis on retinal proteins
Structure determination of ?–helical membrane proteins by solution-state NMR: Emphasis on retinal proteins
Publication date: Available online 2 July 2013
Source:Biochimica et Biophysica Acta (BBA) - Bioenergetics</br>
Author(s): Antoine Gautier</br>
The biochemical processes of living cells involve a numerous series of reactions that work with exceptional specificity and efficiency. The tight control of this intricate reaction network stems from the architecture of the proteins that drive the chemical reactions and mediate protein–protein interactions. Indeed, the...
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07-02-2013 09:44 AM
Requirements on Paramagnetic Relaxation Enhancement Data for Membrane Protein Structure Determination by NMR
Requirements on Paramagnetic Relaxation Enhancement Data for Membrane Protein Structure Determination by NMR
6 June 2012
Publication year: 2012
Source:Structure, Volume 20, Issue 6</br>
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Nuclear magnetic resonance (NMR) structure calculations of the ?-helical integral membrane proteins DsbB, GlpG, and halorhodopsin show that distance restraints from paramagnetic relaxation enhancement (PRE) can provide sufficient structural information to determine their structure with an accuracy of about 1.5*Å in the absence of other long-range conformational restraints. Our...
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02-03-2013 10:13 AM
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
Solid-State NMR of a Large Membrane Protein by Paramagnetic Relaxation Enhancement.
J Phys Chem Lett. 2011 Jul 21;2(14):1836-1841
Authors: Tang M, Berthold DA, Rienstra CM
Membrane proteins play an important role in many biological functions. Solid-state NMR spectroscopy is uniquely suited for studying structure and dynamics of membrane proteins in a membranous environment. The major challenge to obtain high quality solid-state NMR spectra of membrane proteins is...
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08-16-2011 01:19 PM
Solution NMR studies of polytopic ?-helical membrane proteins.
Solution NMR studies of polytopic ?-helical membrane proteins.
Solution NMR studies of polytopic ?-helical membrane proteins.
Curr Opin Struct Biol. 2011 Jul 18;
Authors: Nietlispach D, Gautier A
NMR spectroscopy has established itself as one of the main techniques for the structural study of integral membrane proteins. Remarkably, over the last few years, substantial progress has been achieved in the structure determination of increasingly complex polytopical ?-helical membrane proteins, with their size approaching ~100kDa. Such advances are the...
Solution NMR Structure Determination of Polytopic ?-Helical Membrane Proteins: A Guide to Spin Label Paramagnetic Relaxation Enhancement Restraints.
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