The combination of chemical shift, residual dipolar coupling, and backbone relaxation data can be used to characterize the nature of a domain interface in a multidomain protein. Comparison of the parameters obtained from isolated domains and domain pairs provides insight into the composition of the interface as well as into interdomain dynamics. The interface between the 13th and 14th F3 module from fibronectin is used as an example.
[NMR paper] An NMR method for the determination of protein-binding interfaces using dioxygen-indu
An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement.
Related Articles An NMR method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement.
J Am Chem Soc. 2005 Apr 27;127(16):5826-32
Authors: Sakakura M, Noba S, Luchette PA, Shimada I, Prosser RS
Using oxygen as a paramagnetic probe, researchers can routinely study topologies and protein-binding interfaces by NMR. The paramagnetic contribution to the amide (1)H...
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11-25-2010 08:21 PM
[NMR paper] High-pressure NMR spectroscopy for characterizing folding intermediates and denatured
High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.
Related Articles High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins.
Methods. 2004 Sep;34(1):133-43
Authors: Kamatari YO, Kitahara R, Yamada H, Yokoyama S, Akasaka K
Extensive structural studies using high-pressure NMR spectroscopy have recently been carried out on proteins, which potentially contribute to our understanding of the mechanisms of protein folding. Pressure shifts the...
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[NMR paper] NMR-based metabolomics: a powerful approach for characterizing the effects of environ
NMR-based metabolomics: a powerful approach for characterizing the effects of environmental stressors on organism health.
Related Articles NMR-based metabolomics: a powerful approach for characterizing the effects of environmental stressors on organism health.
Environ Sci Technol. 2003 Nov 1;37(21):4982-9
Authors: Viant MR, Rosenblum ES, Tieerdema RS
It is important to assess the chronic effects of chemical, physical, and biological stressors on organisms in the environment. Appropriate methods must enable rapid, inexpensive, and...
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11-24-2010 09:16 PM
[NMR paper] Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the
Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA.
Related Articles Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA.
J Biomol NMR. 1998 Jul;12(1):51-71
Authors: Foster MP, Wuttke DS, Clemens KR, Jahnke W, Radhakrishnan I, Tennant L, Reymond M, Chung J, Wright PE
We report the NMR resonance assignments for a macromolecular...
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Scientist develops new, innovative methods for characterizing proteins - Eureka! Scie
Scientist develops new, innovative methods for characterizing proteins - Eureka! Science News
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Eureka! Science News
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Scientist develops new, innovative methods for characterizing proteins
Eureka! Science News
Nuclear magnetic resonance (NMR) data are first collected for a particular protein that is being analyzed. (NMR is a research tool that utilizes high ...
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[NMR paper] A 1H NMR comparative study of the structure of the critical packing interfaces betwee
A 1H NMR comparative study of the structure of the critical packing interfaces between helix and non-helical region in various ligation states of sperm whale myoglobin.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A 1H NMR comparative study of the structure of the critical packing interfaces between helix and non-helical region in various ligation states of sperm whale myoglobin.
Biochim Biophys Acta. 1997 Nov 14;1343(1):59-66
Authors: Yamamoto Y
NMR signals arising...
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[NMR paper] Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N a
Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
J Mol Biol. 1996 Dec 20;264(5):1101-16
Authors: Venters RA, Farmer BT, Fierke CA, Spicer LD
Perdeuteration of all non-exchangeable proton sites can...
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08-22-2010 02:20 PM
Structural determination of biomolecular interfaces by nuclear magnetic resonance of
Abstract Protein interactions are important for understanding many molecular mechanisms underlying cellular processes. So far, interfaces between interacting proteins have been characterized by NMR spectroscopy mostly by using chemical shift perturbations and cross-saturation via intermolecular cross-relaxation. Although powerful, these techniques cannot provide unambiguous estimates of intermolecular distances between interacting proteins. Here, we present an alternative approach, called REDSPRINT (REDduced/Standard PRoton density INTerface identification), to map protein interfaces with...
Characterizing domain interfaces by NMR.
Linear Mode
