Related ArticlesNMR structure of the 18 kDa protein CC1736 from Caulobacter crescentus identifies a member of the START domain superfamily and suggests residues mediating substrate specificity.
Proteins. 2005 Feb 15;58(3):747-50
Authors: Shen Y, Goldsmith-Fischman S, Atreya HS, Acton T, Ma L, Xiao R, Honig B, Montelione GT, Szyperski T
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Related Articles Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Structure. 2010 Dec 8;18(12):1678-1687
Authors: Masica DL, Ash JT, Ndao M, Drobny GP, Gray JJ
Protein-biomineral interactions are paramount to materials production in biology, including the mineral phase of hard tissue. Unfortunately, the...
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[NMR paper] NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural di
NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.
Related Articles NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.
J Biol Chem. 2005 Jun 17;280(24):22582-9
Authors: Howard MJ, Smales CM
The non-enzymatic reaction between reducing sugars and long-lived proteins in vivo results in the formation of glycation and advanced glycation end products, which alter the properties of proteins including charge,...
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[NMR paper] NMR structure note--solution structure of a bacterial BolA-like protein XC975 from a
NMR structure note--solution structure of a bacterial BolA-like protein XC975 from a plant pathogen Xanthomonas campestris pv. campestris.
Related Articles NMR structure note--solution structure of a bacterial BolA-like protein XC975 from a plant pathogen Xanthomonas campestris pv. campestris.
J Biomol NMR. 2005 Feb;31(2):167-72
Authors: Chin KH, Lin FY, Hu YC, Sze KH, Lyu PC, Chou SH
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[NMR paper] Multidimensional NMR identifies the conformational shift essential for catalytic comp
Multidimensional NMR identifies the conformational shift essential for catalytic competence in the 60-kDa Drosophila melanogaster dUTPase trimer.
Related Articles Multidimensional NMR identifies the conformational shift essential for catalytic competence in the 60-kDa Drosophila melanogaster dUTPase trimer.
J Biol Chem. 2004 Apr 23;279(17):17945-50
Authors: Dubrovay Z, Gáspári Z, Hunyadi-Gulyás E, Medzihradszky KF, Perczel A, Vértessy BG
The catalytic mechanism of dUTP pyrophosphatase (dUTPase), responsible for the prevention of uracil...
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[NMR paper] Structure prediction of protein complexes by an NMR-based protein docking algorithm.
Structure prediction of protein complexes by an NMR-based protein docking algorithm.
Related Articles Structure prediction of protein complexes by an NMR-based protein docking algorithm.
J Biomol NMR. 2001 May;20(1):15-21
Authors: Kohlbache O, Burchardt A, Moll A, Hildebrandt A, Bayer P, Lenhof HP
Protein docking algorithms can be used to study the driving forces and reaction mechanisms of docking processes. They are also able to speed up the lengthy process of experimental structure elucidation of protein complexes by proposing potential...
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11-19-2010 08:32 PM
[NMR paper] How do the x-ray structure and the NMR structure of FMN-binding protein differ?
How do the x-ray structure and the NMR structure of FMN-binding protein differ?
Related Articles How do the x-ray structure and the NMR structure of FMN-binding protein differ?
Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):368-71
Authors: Suto K, Kawagoe K, Shibata N, Morimoto Y, Higuchi Y, Kitamura M, Nakaya T, Yasuoka N
The crystal structure of FMN-binding protein (FMN-bp) from Desulfovibrio vulgaris Miyazaki F was solved by the multiple isomorphous replacement method and refined to an R factor of 15.1% at 1.3 A resolution. FMN-bp...
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NMR structure of the protein NP_247299.1: comparison with the crystal structure.
NMR structure of the protein NP_247299.1: comparison with the crystal structure.
Related Articles NMR structure of the protein NP_247299.1: comparison with the crystal structure.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1367-80
Authors: Jaudzems K, Geralt M, Serrano P, Mohanty B, Horst R, Pedrini B, Elsliger MA, Wilson IA, Wüthrich K
The NMR structure of the protein NP_247299.1 in solution at 313 K has been determined and is compared with the X-ray crystal structure, which was also solved in the Joint Center for...
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[NMR paper] NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein
NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
Biochemistry. 1997 Sep 2;36(35):10709-17
Authors: Xu RX, Pawelczyk T, Xia TH, Brown SC
Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich...
NMR structure of the 18 kDa protein CC1736 from Caulobacter crescentus identifies a m
Linear Mode
