An automated iterative approach for protein structure refinement using pseudocontact shifts
An automated iterative approach for protein structure refinement using pseudocontact shifts
Abstract
NMR structure calculation using NOE-derived distance restraints requires a considerable number of assignments of both backbone and sidechains resonances, often difficult or impossible to get for large or complex proteins. Pseudocontact shifts (PCSs) also play a well-established role in NMR protein structure calculation, usually to augment existing structural, mostly NOE-derived, information. Existing refinement protocols using PCSs usually either...
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[NMR paper] Correction to: Joint X-ray/NMR structure refinement of multidomain/multisubunit systems.
Correction to: Joint X-ray/NMR structure refinement of multidomain/multisubunit systems.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Correction to: Joint X-ray/NMR structure refinement of multidomain/multisubunit systems.
J Biomol NMR. 2019 May 08;:
Authors: Carlon A, Ravera E, Parigi G, Murshudov GN, Luchinat C
Abstract
The article "Joint X-ray/NMR structure refinement of multidomain/multisubunit systems" written by...
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05-11-2019 07:56 PM
Correction to: Joint X-ray/NMR structure refinement of multidomain/multisubunit systems
Correction to: Joint X-ray/NMR structure refinement of multidomain/multisubunit systems
The article â??Joint X-ray/NMR structure refinement of multidomain/multisubunit systemsâ?? written by â??Azzurra Carlon, Enrico Ravera, Giacomo Parigi, Garib N. Murshudov and Claudio Luchinatâ?? was originally published electronically on the publisherâ??s internet portal (currently SpringerLink) on 11 October 2018 without open access.
Source: Journal of Biomolecular NMR
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Integral membrane protein structure determination using pseudocontact shifts
Integral membrane protein structure determination using pseudocontact shifts
Abstract
Obtaining enough experimental restraints can be a limiting factor in the NMR structure determination of larger proteins. This is particularly the case for large assemblies such as membrane proteins that have been solubilized in a membrane-mimicking environment. Whilst in such cases extensive deuteration strategies are regularly utilised with the aim to improve the spectral quality, these schemes often limit the number of NOEs obtainable, making complementary...
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01-21-2015 08:39 PM
Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution
Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution
Abstract Random coil chemical shifts are necessary for secondary chemical shift analysis, which is the main NMR method for identification of secondary structure in proteins. One of the largest challenges in the determination of random coil chemical shifts is accounting for the effect of neighboring residues. The contributions from the neighboring residues are typically removed by using neighbor correction factors determined based on each...
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06-06-2011 12:53 AM
[NMR paper] The impact of direct refinement against proton chemical shifts on protein structure d
The impact of direct refinement against proton chemical shifts on protein structure determination by NMR.
Related Articles The impact of direct refinement against proton chemical shifts on protein structure determination by NMR.
J Magn Reson B. 1995 Jun;107(3):293-7
Authors: Kuszewski J, Gronenborn AM, Clore GM
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[NMR paper] Protein structure refinement based on paramagnetic NMR shifts: applications to wild-t
Protein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Protein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c.
Protein Sci. 1995 Feb;4(2):296-305
...
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[NMR paper] "Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applie
"Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applied to the solution structure of crambin.
Related Articles "Ensemble" iterative relaxation matrix approach: a new NMR refinement protocol applied to the solution structure of crambin.
Proteins. 1993 Apr;15(4):385-400
Authors: Bonvin AM, Rullmann JA, Lamerichs RM, Boelens R, Kaptein R
The structure in solution of crambin, a small protein of 46 residues, has been determined from 2D NMR data using an iterative relaxation matrix approach (IRMA) together with...
Correction to: An automated iterative approach for protein structure refinement using pseudocontact shifts
Linear Mode
