Related ArticlesSolution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectroscopy.
Biochemistry. 1996 Mar 5;35(9):2845-53
Authors: Jaishree TN, Ramakrishnan V, White SW
The solution of a primary 16S rRNA-binding ribosomal protein, S17, was investigated by two- and three-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. Almost complete chemical shift assignments for the 1H, 15N, and 13C resonances have been obtained. The NMR data have been rigorously analyzed using a combination of distance geometry, back-calculation, and simulated annealing refinement techniques, and a high-resolution three-dimensional structure has been deduced. The protein consists of a single twisted antiparallel beta-pleated sheet with Greek-key topology. The five beta-strands are connected by extended loops that are flexible compared to the beta-sheet core structure and appear not to adopt one definite conformation in solution. Two of these loops contain many of the residues that have been implicated in binding ribosomal RNA. The location and distribution of these residues and other positively charged side chains on the protein surface suggest an interaction with two distinct regions of ribosomal RNA.
[NMR paper] The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARC
The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein fold.
Related Articles The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein fold.
Protein Sci. 2004 May;13(5):1407-16
Authors: Herve du Penhoat C, Atreya HS, Shen Y, Liu G, Acton TB, Xiao R, Li Z, Murray D, Montelione GT, Szyperski T
The Archaeoglobus fulgidis gene RS27_ARCFU encodes the 30S ribosomal protein S27e. Here, we...
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[NMR paper] Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Related Articles Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Protein Sci. 2003 Dec;12(12):2823-30
Authors: Aramini JM, Huang YJ, Cort JR, Goldsmith-Fischman S, Xiao R, Shih LY, Ho CK, Liu J, Rost B, Honig B, Kennedy MA, Acton TB, Montelione GT
We report NMR assignments and solution structure of the 71-residue 30S ribosomal protein S28E from the archaean Pyrococcus horikoshii, target JR19 of the Northeast Structural...
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[NMR paper] High-resolution solution NMR structure of the minimal active domain of the human immu
High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Related Articles High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Biochemistry. 1998 Dec 22;37(51):17704-13
Authors: Kodera Y, Sato K, Tsukahara T, Komatsu H, Maeda T, Kohno T
The retroviral nucleocapsid (NC) protein is a multifunctional protein essential for RNA genome packaging and viral infectivity. The NC protein, NCp8, of the...
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[NMR paper] High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles High-resolution solution NMR structure of the Z domain of staphylococcal protein A.
J Mol Biol. 1997 Oct 3;272(4):573-90
Authors: Tashiro M, Tejero R, Zimmerman DE, Celda B, Nilsson B, Montelione GT
Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size...
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[NMR paper] High resolution NMR solution structure of the leucine zipper domain of the c-Jun homo
High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.
J Biol Chem. 1996 Jun 7;271(23):13663-7
Authors: Junius FK, O'Donoghue SI, Nilges M, Weiss AS, King GF
The solution structure of the c-Jun leucine zipper domain has been determined to high resolution using a new...
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[NMR paper] Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spec
Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy.
Related Articles Solution structure of the phosphorylated sites of ribosomal protein S6 by 1H NMR spectroscopy.
Int J Pept Protein Res. 1996 Apr;47(4):282-8
Authors: Katahira R, Flotow H, Thomas G, Nosaka AY
An increase in the rate of protein synthesis is found to be accompanied by phosphorylation of the 40S ribosomal protein S6. Treatment of S6 by cyanogen bromide produced three fragments, and one of the fragments of S6, which is a C-terminal...
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[NMR paper] Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR
Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing.
Related Articles Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing.
Biochemistry. 1994 May 31;33(21):6408-17
Authors: Qi PX, Di Stefano DL, Wand AJ
A model for the solution structure of horse heart ferrocytochrome c has been determined by nuclear magnetic resonance spectroscopy combined with hybrid distance geometry-simulated annealing calculations....
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[NMR paper] Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR
Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing.
Related Articles Solution structure of horse heart ferrocytochrome c determined by high-resolution NMR and restrained simulated annealing.
Biochemistry. 1994 May 31;33(21):6408-17
Authors: Qi PX, Di Stefano DL, Wand AJ
A model for the solution structure of horse heart ferrocytochrome c has been determined by nuclear magnetic resonance spectroscopy combined with hybrid distance geometry-simulated annealing calculations....
Solution structure of prokaryotic ribosomal protein S17 by high-resolution NMR spectr
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