Related ArticlesDirect determination of changes of interdomain orientation on ligation: use of the orientational dependence of 15N NMR relaxation in Abl SH(32).
Biochemistry. 1999 Aug 10;38(32):10225-30
Authors: Fushman D, Xu R, Cowburn D
The relative orientation and motions of domains within many proteins are key to the control of multivalent recognition, or the assembly of protein-based cellular machines. Current methods of structure determination have limited applicability to macromolecular assemblies, characterized by weak interactions between the constituents. Crystal structures of such complexes might be biased by packing forces comparable to the interdomain interactions, while the precision and accuracy of the conventional NMR structural approaches are necessarily limited by the restricted number of NOE contacts and by interdomain flexibility rendering the available NOE information uninterpretable. NMR relaxation studies are capable of providing "long-range" structural information on macromolecules in their native milieu. Here we determine directly the change in domain orientation between unligated and dual ligated subdomains of the SH(32) segment of Abelson kinase in solution, using the orientational dependence of nuclear spin relaxation. These results demonstrate that the change in domain orientation between unligated and ligated forms can be measured directly in solution.
Direct NMR Observationand pKa Determination of the Asp102 Side Chain in a SerineProtease
Direct NMR Observationand pKa Determination of the Asp102 Side Chain in a SerineProtease
Paul Everill, James L. Sudmeier and William W. Bachovchin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210091q/aop/images/medium/ja-2011-10091q_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja210091q
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Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
Impact of (15)N R(2)/R(1) Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints.
J Am Chem Soc. 2011 Apr 4;
Authors: Ryabov Y, Schwieters CD, Clore GM
(15)N R(2)/R(1) relaxation data contain information on molecular shape and size as well as on bond vector orientations relative to...
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Impact of 15N R2/R1 Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints
Impact of 15N R2/R1 Relaxation Restraints on Molecular Size, Shape, and Bond Vector Orientation for NMR Protein Structure Determination with Sparse Distance Restraints
Yaroslav Ryabov, Charles D. Schwieters and G. Marius Clore
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja201020c/aop/images/medium/ja-2011-01020c_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja201020c
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[NMR paper] Direct determination of the interleukin-6 binding epitope of the interleukin-6 recept
Direct determination of the interleukin-6 binding epitope of the interleukin-6 receptor by NMR spectroscopy.
Related Articles Direct determination of the interleukin-6 binding epitope of the interleukin-6 receptor by NMR spectroscopy.
J Biol Chem. 2004 Jan 2;279(1):571-6
Authors: Schwantner A, Dingley AJ, Ozbek S, Rose-John S, Grötzinger J
All cytokines belonging to the interleukin-6 (IL-6)-type family of cytokines utilize receptors that have a modular build of several immunoglobulin-like and fibronectin type III-like domains. Characteristic...
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[NMR paper] Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
Related Articles Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
J Am Chem Soc. 2001 May 2;123(17):3953-9
Authors: Baber JL, Szabo A, Tjandra N
The interpretation of NMR relaxation data for macromolecules possessing slow interdomain motions is considered. It is shown how the "extended model-free approach" can be used to analyze (15)N backbone relaxation data acquired at three different field strengths for Xenopus Ca(2+)-ligated...
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[NMR paper] Toward direct determination of conformations of protein building units from multidime
Toward direct determination of conformations of protein building units from multidimensional NMR experiments part II: a theoretical case study of formyl-L-valine amide.
Related Articles Toward direct determination of conformations of protein building units from multidimensional NMR experiments part II: a theoretical case study of formyl-L-valine amide.
Chemistry. 2001 Mar 2;7(5):1069-83
Authors: Perczel A, Császár AG
Chemical shielding anisotropy tensors have been determined for all twenty-seven characteristic conformers of For-L-Val-NH2 using...
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[NMR paper] A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain reg
A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles A proton-NMR study of a site-directed mutation (His388----Glu) in the interdomain region of yeast phosphoglycerate kinase. Implications for domain movement.
Eur J Biochem. 1991 Mar 14;196(2):261-9
Authors: Graham HC, Williams RJ, Littlechild...
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[NMR paper] NMR determination of the orientation of the magnetic susceptibility tensor in cyanome
NMR determination of the orientation of the magnetic susceptibility tensor in cyanometmyoglobin: a new probe of steric tilt of bound ligand.
Related Articles NMR determination of the orientation of the magnetic susceptibility tensor in cyanometmyoglobin: a new probe of steric tilt of bound ligand.
Biochemistry. 1990 Feb 13;29(6):1556-66
Authors: Emerson SD, La Mar GN
The experimentally determined paramagnetic dipolar shifts for noncoordinated amino acid side-chain protons in the heme pocket of sperm whale cyanometmyoglobin ) were used to...