Related ArticlesCorrection: Fragment density functional theory calculation of NMR chemical shifts for proteins with implicit solvation.
Phys Chem Chem Phys. 2015 Apr 21;
Authors: Zhu T, He X, Zhang JZ
Abstract
Correction for 'Fragment density functional theory calculation of NMR chemical shifts for proteins with implicit solvation' by Tong Zhu et al., Phys. Chem. Chem. Phys., 2012, 14, 7837-7845.
PMID: 25897947 [PubMed - as supplied by publisher]
[NMR paper] Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts.
Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts.
Related Articles Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts.
Proc Natl Acad Sci U S A. 2014 Sep 5;
Authors: Boomsma W, Tian P, Frellsen J, Ferkinghoff-Borg J, Hamelryck T, Lindorff-Larsen K, Vendruscolo M
Abstract
Methods of protein structure determination based on NMR chemical shifts are becoming increasingly common. The most widely used approaches adopt the molecular...
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09-07-2014 12:36 PM
[NMR paper] A practical implicit solvent potential for NMR structure calculation.
A practical implicit solvent potential for NMR structure calculation.
Related Articles A practical implicit solvent potential for NMR structure calculation.
J Magn Reson. 2014 Apr 2;243C:54-64
Authors: Tian Y, Schwieters CD, Opella SJ, Marassi FM
Abstract
The benefits of protein structure refinement in water are well documented. However, performing structure refinement with explicit atomic representation of the solvent molecules is computationally expensive and impractical for NMR-restrained structure calculations that start from...
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04-22-2014 03:54 PM
[NMR paper] A Practical Implicit Solvent Potential for NMR Structure Calculation
A Practical Implicit Solvent Potential for NMR Structure Calculation
Publication date: Available online 2 April 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Ye Tian , Charles D. Schwieters , Stanley J. Opella , Francesca M. Marassi</br>
The benefits of protein structure refinement in water are well documented. However, performing structure refinement with explicit atomic representation of the solvent molecules is computationally expensive and impractical for NMR-restrained structure calculations that start from completely extended polypeptide...
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
Addressing the Stereochemistry of Complex Organic Molecules by Density Functional Theory-NMR: Vannusal B in Retrospective
Addressing the Stereochemistry of Complex Organic Molecules by Density Functional Theory-NMR: Vannusal B in Retrospective
Giacomo Saielli, K. C. Nicolaou, Adrian Ortiz, Hongjun Zhang and Alessandro Bagno
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201108a/aop/images/medium/ja-2011-01108a_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201108a
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/hTB3xm5f79k
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03-25-2011 08:21 PM
[NMR paper] Sequence-dependent correction of random coil NMR chemical shifts.
Sequence-dependent correction of random coil NMR chemical shifts.
Related Articles Sequence-dependent correction of random coil NMR chemical shifts.
J Am Chem Soc. 2001 Apr 4;123(13):2970-8
Authors: Schwarzinger S, Kroon GJ, Foss TR, Chung J, Wright PE, Dyson HJ
Random coil chemical shifts are commonly used to detect secondary structure elements in proteins in chemical shift index calculations. While this technique is very reliable for folded proteins, application to unfolded proteins reveals significant deviations from measured random coil...
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11-19-2010 08:32 PM
Density functional calculations of 15N chemical shifts in solvated dipeptides
Density functional calculations of 15N chemical shifts in solvated dipeptides
Ling Cai, David Fushman and Daniel S. Kosov
Journal of Biomolecular NMR; 2008; 41(2) pp 77 - 88
Abstract:
We performed density functional calculations to examine the effects of solvation, hydrogen bonding, backbone conformation, and the side chain on 15N chemical shielding in proteins. We used N-methylacetamide (NMA) and N-formyl-alanyl-X (with X being one of the 19 naturally occurring amino acids excluding proline) as model systems. In addition, calculations were performed for selected fragments from...
Correction: Fragment density functional theory calculation of NMR chemical shifts for proteins with implicit solvation.
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