Structure determination of protein complexes by NMR.

Structure determination of protein complexes by NMR. Research Abstract Details 

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Structure determination of protein complexes by NMR. Abstract Text:

Daniel Nietlispach,Helen R Mott,Katherine M Stott,Peter R Nielsen,Abarna Thiru,Ernest D Laue,

This chapter describes nuclear magnetic resonance (NMR) methods that can be used to determine the structures of protein complexes. Many of these techniques are also applicable to other systems (e.g., protein-nucleic acid complexes). In the first section, we discuss methodologies for optimizing the sample conditions for the study of complexes. This is followed by a description of the methods that can be used to map interfaces when a full structure determination of the complex is not appropriate or not possible. We then describe experimental approaches for resonance assignment in complexes, these are essentially the same as those for isolated proteins. Subheading 6. describes the different types of so-called X-filtered NMR experiments that have been devised to separate and selectively observe either inter- or intramolecular structural information. These filtered NMR experiments are then exploited in the experimental strategies for structure determination of either protein complexes or homodimeric proteins. This is followed by a description of the calculation of their structures. Finally, we present case studies from three projects carried out in our laboratory, where we successfully used the methods presented in this chapter.

Structure determination of protein complexes by NMR. Publishing Authors By Initials

D Nietlispach,HR Mott,KM Stott,PR Nielsen,A Thiru,ED Laue,

For similar enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: p21-activated kinases research abstracts see: enzymes and coenzymes: enzymes: transferases: phosphotransferases: phosphotransferases (alcohol group acceptor): protein kinases: protein-serine-threonine kinases: p21-activated kinases research

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Structure determination of protein complexes by NMR. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Methods in molecular biology (Clifton, N.J.)

VOLUME: 278

Page Numbers: 255-88

Journal Abbreviation: Methods Mol. Biol.

ISSN: 1064-3745

DAY: 19

MONTH: 11

YEAR: 2004

Structure determination of protein complexes by NMR. Information

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LANGUAGE: eng

NlmUniqueID: 9214969

Structure determination of protein complexes by NMR. Keywords Mesh Terms:

KEYWORDS: p21-Activated Kinases

MESH TERMS: chemistry

Chemical & Substance for Abstract: Structure determination of protein complexes by NMR. Information

Substance Name: GTP-Binding Proteins

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Structure determination of protein complexes by NMR.

AFFILIATION: Department of Biochemistry, University of Cambridge, UK.

Country: United States

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MEDLINETA: Methods Mol Biol

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