Related ArticlesMultidimensional NMR spectroscopy of DNA-binding proteins: structure and function of a transcription factor.
Toxicol Lett. 1995 Dec;82-83:577-89
Authors: Hsu VL, Jia X, Kearns DR
The solution structure of a type II DNA-binding protein (DBPII), transcription factor 1 (TF1), has been determined using NMR spectroscopy. A multidimensional, heteronuclear strategy was employed to overcome assignment ambiguities due to resonance overlap and broadened crosspeaks. This approach involved the use of selectively deuteriated, 13C- and 15N-labeled samples and 'isotopic heterodimers' to distinguish between intra- and intermonomeric NOEs. A comparison with the crystal structure and NMR analysis of the E. coli HU protein suggests that other homologous proteins in this family will possess similar tertiary structures. This NMR strategy is applicable to the study of other proteins and their biomolecular complexes.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Solution NMR structure of VF0530 from Vibrio fischeri reveals a nucleic acid-binding function.
Proteins. 2011 Oct;79(10):2988-91
Authors: Aramini JM, Rossi P, Fischer M, Xiao R, Acton TB, Montelione GT
Abstract
Protein domain family PF09905 (DUF2132) is a family of small domains of unknown function that are conserved in a wide range of bacteria. Here we describe the solution NMR structure of the 80-residue VF0530 protein from Vibrio fischeri,...
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[NMR paper] Cofactor fingerprinting with STD NMR to characterize proteins of unknown function: id
Cofactor fingerprinting with STD NMR to characterize proteins of unknown function: identification of a rare cCMP cofactor preference.
Related Articles Cofactor fingerprinting with STD NMR to characterize proteins of unknown function: identification of a rare cCMP cofactor preference.
FEBS Lett. 2005 Jan 31;579(3):661-6
Authors: Yao H, Sem DS
Proteomics efforts have created a need for better strategies to functionally categorize newly discovered proteins. To this end, we have employed saturation transfer difference NMR with pools of closely...
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[NMR paper] Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins u
Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
Related Articles Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection.
J Am Chem Soc. 2003 Oct 1;125(39):11816-7
Authors: Duma L, Hediger S, Brutscher B, Böckmann A, Emsley L
We show that the resolution of homonuclear multidimensional solid-state NMR correlation experiments can be significantly improved using transition selection and spin-state-selective polarization transfer...
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[NMR paper] Structure and function of HIV-1 and SIV Tat proteins based on carboxy-terminal trunca
Structure and function of HIV-1 and SIV Tat proteins based on carboxy-terminal truncations, chimeric Tat constructs, and NMR modeling.
Related Articles Structure and function of HIV-1 and SIV Tat proteins based on carboxy-terminal truncations, chimeric Tat constructs, and NMR modeling.
Biomed Pharmacother. 1998;52(10):421-30
Authors: Baier-Bitterlich G, Tretiakova A, Richardson MW, Khalili K, Jameson B, Rappaport J
To further define the structure and function of the domains in HIV-1 and SIV Tat proteins, chimeric Tat cDNA expression constructs...
[NMR paper] Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escheri
Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli.
Related Articles Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli.
J Biomol NMR. 1992 Mar;2(2):149-60
Authors: Tjandra N, Simplaceanu V, Cottam PF, Ho C
Specific and uniform 15N labelings along with site-directed mutagenesis of glutamine-binding protein have been utilized to obtain assignments of the His156, Trp32 and Trp220 residues. These assignments have been made not only to further study the...
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[NMR paper] Triple-resonance multidimensional NMR study of calmodulin complexed with the binding
Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.
Related Articles Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle myosin light-chain kinase: indication of a conformational change in the central helix.
Biochemistry. 1991 Jun 4;30(22):5498-504
Authors: Ikura M, Kay LE, Krinks M, Bax A
Heteronuclear 3D and 4D NMR experiments have been...
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Structure and function of G protein-coupled receptors using NMR spectroscopy
Structure and function of G protein-coupled receptors using NMR spectroscopy
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 12 May 2010</br>
Joseph A., Goncalves , Shivani, Ahuja , Sina, Erfani , Markus, Eilers , Steven O., Smith</br>
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Multidimensional NMR spectroscopy of DNA-binding proteins: structure and function of
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