Related ArticlesAn 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 spin-lattice relaxation rates (R(1)(P)) have been studied for uniformly (2)H,(15)N-labeled FB protein, a 60-residue three-helix bundle, constituting the B domain of protein A. Through TROSY versions of inversion-recovery experiments, R(1)(P) could be determined. R(1)(P) was then measured in the presence of a stoichiometric equivalent of an unlabeled Fc fragment of immunoglobulin (Ig) G, and the ratio of R(1)(P) of the FB-Fc complex to that of free FB [i.e., R(1)(P)(complex)/R(1)(P)(free)] was determined for each observable residue. Regions of helix I and helix II, which were previously known to interact with Fc, were readily identified as belonging to the binding interface by their characteristically reduced values of R(1)(P)(complex)/R(1)(P)(free). The method of comparing oxygen-induced spin-lattice relaxation rates of free protein and protein-protein complexes, to detect binding interfaces, offers greater sensitivity than chemical shift perturbation, while it is not necessary to heavily deuterate the labeled protein, as is the case in cross saturation experiments.
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Related Articles Toward a Structure Determination Method for Biomineral-Associated Protein Using Combined Solid- State NMR and Computational Structure Prediction.
Structure. 2010 Dec 8;18(12):1678-1687
Authors: Masica DL, Ash JT, Ndao M, Drobny GP, Gray JJ
Protein-biomineral interactions are paramount to materials production in biology, including the mineral phase of hard tissue. Unfortunately, the...
nmrlearner
Journal club
0
12-08-2010 06:21 PM
[NMR paper] High-throughput inference of protein-protein interfaces from unassigned NMR data.
High-throughput inference of protein-protein interfaces from unassigned NMR data.
Related Articles High-throughput inference of protein-protein interfaces from unassigned NMR data.
Bioinformatics. 2005 Jun;21 Suppl 1:i292-301
Authors: Mettu RR, Lilien RH, Donald BR
SUMMARY: We cast the problem of identifying protein-protein interfaces, using only unassigned NMR spectra, into a geometric clustering problem. Identifying protein-protein interfaces is critical to understanding inter- and intra-cellular communication, and NMR allows the study of...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Fast mapping of protein-protein interfaces by NMR spectroscopy.
Fast mapping of protein-protein interfaces by NMR spectroscopy.
Related Articles Fast mapping of protein-protein interfaces by NMR spectroscopy.
J Am Chem Soc. 2003 Nov 26;125(47):14250-1
Authors: Reese ML, Dötsch V
Identifying the interface of protein complexes can represent a difficult task in structural biology. Here, we report a method for the fast mapping of interfaces of protein complexes by NMR without the need for the assignments of the proteins involved.
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] A novel NMR method for determining the interfaces of large protein-protein complexes.
A novel NMR method for determining the interfaces of large protein-protein complexes.
Related Articles A novel NMR method for determining the interfaces of large protein-protein complexes.
Nat Struct Biol. 2000 Mar;7(3):220-3
Authors: Takahashi H, Nakanishi T, Kami K, Arata Y, Shimada I
Identification of the interfaces of large (Mr > 50,000) protein-protein complexes in solution by high resolution NMR has typically been achieved using experiments involving chemical shift perturbation and/or hydrogen-deuterium exchange of the main chain amide...
nmrlearner
Journal club
0
11-18-2010 09:15 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...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] NMR structure determination of the binding site for ribosomal protein S8 from Escheri
NMR structure determination of the binding site for ribosomal protein S8 from Escherichia coli 16 S rRNA.
Related Articles NMR structure determination of the binding site for ribosomal protein S8 from Escherichia coli 16 S rRNA.
J Mol Biol. 1998 Jul 24;280(4):639-54
Authors: Kalurachchi K, Nikonowicz EP
Many cellular processes involve the preferential interaction of an RNA molecule with a specific protein. A detailed analysis of the individual protein and RNA components of these interactions can provide unique insights into the structural...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] NMR - this other method for protein and nucleic acid structure determination.
NMR - this other method for protein and nucleic acid structure determination.
Related Articles NMR - this other method for protein and nucleic acid structure determination.
Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):249-70
Authors: Wüthrich K
For a quarter of a century X-ray diffraction in single crystals was unique in its ability to solve three-dimensional structures of proteins and nucleic acids at atomic resolution. The situation changed in 1984 with the completion of a protein structure determination by nuclear magnetic...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
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...
An NMR method for the determination of protein-binding interfaces using dioxygen-indu
Linear Mode
