Protein complexes studied by NMR spectroscopy

doi:10.1016/s0958-1669(96)80115-7

Review

. 1996 Aug;7(4):403-8.

doi: 10.1016/s0958-1669(96)80115-7.

Protein complexes studied by NMR spectroscopy

A J Wand¹, S W Englander

Affiliations

PMID: 8768898
PMCID: PMC3442359
DOI: 10.1016/s0958-1669(96)80115-7

Review

Protein complexes studied by NMR spectroscopy

A J Wand et al. Curr Opin Biotechnol. 1996 Aug.

. 1996 Aug;7(4):403-8.

doi: 10.1016/s0958-1669(96)80115-7.

Authors

A J Wand¹, S W Englander

Affiliation

¹ Department of Biological Sciences, State University of New York at Buffalo 14260, USA. wand@jasper.chem.buffalo.edu

PMID: 8768898
PMCID: PMC3442359
DOI: 10.1016/s0958-1669(96)80115-7

Abstract

Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point where almost any type of complex involving proteins of reasonable size may be studied in a straightforward way. A variety of isotope editing and filtering strategies underlie these powerful methodologies. Approaches to the characterization of the dynamics of protein complexes have also matured to the point where detailed studies of the effects of complexation on dynamics can be studied over a wide range of timescales.

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References

1. Leopold MF, Urbauer JL, Wand AJ. Resonance assignment strategies for the analysis of NMR spectra of proteins. Mol Biotechnol. 1994;2:61–93. - PubMed
1. Clore GM, Gronenborn AM. Structures of larger proteins, protein–ligand and protein–DNA complexes by multidimensional heteronuclear NMR. Prog Biophys Mol Biol. 1994;62:153–184. - PubMed
1. Kay LE. Pulsed field-gradient multidimensional NMR methods for the study of protein structure and dynamics. Prog Biophys Mol Biol. 1995;63:277–299. - PubMed
1. Jarori GK, Murali N, Switzer RL, Rao BD. Conformation of Mg·ATP bound to 5-phospho-alpha-D-ribose 1 -diphosphate synthetase by two-dimensional transferred nuclear Overhauser effect spectroscopy. Eur J Biochem. 1995;230:57–524. A careful application of the transferred NOE technique that pays particular attention to the potential for artifacts arising from nonspecific binding, which may have plagued earlier application of this technique. - PubMed
1. Lian LY, Barsukov IL, Sutcliffe MJ, Sze KH, Roberts GCK. Protein–ligand interactions: exchange processes and determination of ligand conformation and protein–ligand contacts. Methods Enzymol. 1994;239:657–700. - PubMed

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[1] Leopold MF, Urbauer JL, Wand AJ. Resonance assignment strategies for the analysis of NMR spectra of proteins. Mol Biotechnol. 1994;2:61–93. - PubMed

[2] Leopold MF, Urbauer JL, Wand AJ. Resonance assignment strategies for the analysis of NMR spectra of proteins. Mol Biotechnol. 1994;2:61–93. - PubMed

[3] Clore GM, Gronenborn AM. Structures of larger proteins, protein–ligand and protein–DNA complexes by multidimensional heteronuclear NMR. Prog Biophys Mol Biol. 1994;62:153–184. - PubMed

[4] Clore GM, Gronenborn AM. Structures of larger proteins, protein–ligand and protein–DNA complexes by multidimensional heteronuclear NMR. Prog Biophys Mol Biol. 1994;62:153–184. - PubMed

[5] Kay LE. Pulsed field-gradient multidimensional NMR methods for the study of protein structure and dynamics. Prog Biophys Mol Biol. 1995;63:277–299. - PubMed

[6] Kay LE. Pulsed field-gradient multidimensional NMR methods for the study of protein structure and dynamics. Prog Biophys Mol Biol. 1995;63:277–299. - PubMed

[7] Jarori GK, Murali N, Switzer RL, Rao BD. Conformation of Mg·ATP bound to 5-phospho-alpha-D-ribose 1 -diphosphate synthetase by two-dimensional transferred nuclear Overhauser effect spectroscopy. Eur J Biochem. 1995;230:57–524. A careful application of the transferred NOE technique that pays particular attention to the potential for artifacts arising from nonspecific binding, which may have plagued earlier application of this technique. - PubMed

[8] Jarori GK, Murali N, Switzer RL, Rao BD. Conformation of Mg·ATP bound to 5-phospho-alpha-D-ribose 1 -diphosphate synthetase by two-dimensional transferred nuclear Overhauser effect spectroscopy. Eur J Biochem. 1995;230:57–524. A careful application of the transferred NOE technique that pays particular attention to the potential for artifacts arising from nonspecific binding, which may have plagued earlier application of this technique. - PubMed

[9] Lian LY, Barsukov IL, Sutcliffe MJ, Sze KH, Roberts GCK. Protein–ligand interactions: exchange processes and determination of ligand conformation and protein–ligand contacts. Methods Enzymol. 1994;239:657–700. - PubMed

[10] Lian LY, Barsukov IL, Sutcliffe MJ, Sze KH, Roberts GCK. Protein–ligand interactions: exchange processes and determination of ligand conformation and protein–ligand contacts. Methods Enzymol. 1994;239:657–700. - PubMed

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Protein complexes studied by NMR spectroscopy

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Protein complexes studied by NMR spectroscopy

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