Characterization of theConformational Equilibriumbetween the Two Major Substates of RNase A Using NMR Chemical Shifts
Characterization of theConformational Equilibriumbetween the Two Major Substates of RNase A Using NMR Chemical Shifts
Carlo Camilloni, Paul Robustelli, Alfonso De Simone, Andrea Cavalli and Michele Vendruscolo
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Journal of the American Chemical Society
DOI: 10.1021/ja210951z
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Defects in Doped LaGaO3 Anionic Conductors: Linking NMR Spectral Features, Local Environments, and Defect Thermodynamics
Defects in Doped LaGaO3 Anionic Conductors: Linking NMR Spectral Features, Local Environments, and Defect Thermodynamics
Fre?de?ric Blanc, Derek S. Middlemiss, Zhehong Gan and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2053557/aop/images/medium/ja-2011-053557_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2053557
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10-14-2011 08:08 AM
[NMR paper] NMR solution structure, backbone mobility, and homology modeling of c-type cytochrome
NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.
Related Articles NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.
Chembiochem. 2002 Apr 2;3(4):299-310
Authors: Banci L, Bertini I, Ciurli S, Dikiy A, Dittmer J, Rosato A, Sciara G, Thompsett AR
The solution structure of oxidized cytochrome c(553) (71 amino acid residues) from the Gram-positive bacterium Bacillus pasteurii is here reported and compared with the...
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11-24-2010 08:49 PM
[NMR paper] Internal mobility of the basic pancreatic trypsin inhibitor in solution: a comparison
Internal mobility of the basic pancreatic trypsin inhibitor in solution: a comparison of NMR spin relaxation measurements and molecular dynamics simulations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Internal mobility of the basic pancreatic trypsin inhibitor in solution: a comparison of NMR spin relaxation measurements and molecular dynamics simulations.
J Mol Biol. 1995 Feb 17;246(2):356-65
Authors: Smith PE, van Schaik RC, Szyperski T, Wüthrich K, van Gunsteren WF
...
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[NMR paper] Three-dimensional structure in solution of a wheat lipid-transfer protein from multid
Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers.
Eur J Biochem. 1994 Dec 1;226(2):413-22
Authors: Gincel E, Simorre JP, Caille A, Marion D, Ptak M, Vovelle F
...
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[NMR paper] 13C-NMR relaxation study on mobility of the DNA-binding arm of HU.
13C-NMR relaxation study on mobility of the DNA-binding arm of HU.
Related Articles 13C-NMR relaxation study on mobility of the DNA-binding arm of HU.
J Biochem. 1994 Nov;116(5):1153-5
Authors: Kakuta Y, Hojo H, Aimoto S, Tanaka I, Hikichi K
The mobility of the DNA-binding arm of HU protein was studied by 13C-NMR spectroscopy. The correlation times tau c of Phe47C alpha in the body and Gly60C alpha in the arm of HU were determined for HU and HU-DNA complex. The value of tau c of Phe47C alpha is 2-4 times larger than that of Gly60C alpha...
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[NMR paper] NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for
NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21.
Related Articles NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21.
Biochemistry. 1990 Apr 10;29(14):3509-14
Authors: Redfield AG, Papastavros MZ
The structure of the phosphoryl binding region of human N-ras p21 was probed by using heteronuclear proton-observed NMR methods. Normal protein and a Gly-12----Asp-12 mutant protein were prepared...
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08-21-2010 10:48 PM
[NMR paper] Polarization transfer by cross-correlated relaxation in solution NMR with very large
Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules.
Proc Natl Acad Sci U S A. 1999 Apr 27;96(9):4918-23
Authors: Riek R, Wider G, Pervushin K, Wüthrich...
Solution NMR of a 463-ResiduePhosphohexomutase: Domain4 Mobility, Substates, and Phosphoryl Transfer Defect
Linear Mode
