Related ArticlesNMR analysis of the transient complex between membrane photosystem I and soluble cytochrome c6.
J Biol Chem. 2005 Mar 4;280(9):7925-31
Authors: Díaz-Moreno I, Díaz-Quintana A, Molina-Heredia FP, Nieto PM, Hansson O, De la Rosa MA, Karlsson BG
A structural analysis of the surface areas of cytochrome c(6), responsible for the transient interaction with photosystem I, was performed by NMR transverse relaxation-optimized spectroscopy. The hemeprotein was titrated by adding increasing amounts of the chlorophyllic photosystem, and the NMR spectra of the free and bound protein were analyzed in a comparative way. The NMR signals of cytochrome c(6) residues located at the hydrophobic and electrostatic patches, which both surround the heme cleft, were specifically modified by binding. The backbones of internal residues close to the hydrophobic patch of cytochrome c(6) were also affected, a fact that is ascribed to the conformational changes taking place inside the hemeprotein when interacting with photosystem I. To the best of our knowledge, this is the first structural analysis by NMR spectroscopy of a transient complex between soluble and membrane proteins.
Portrayal of complex dynamic properties of sugarcane defensin 5 by NMR: multiple motions associated with membrane interaction.
Portrayal of complex dynamic properties of sugarcane defensin 5 by NMR: multiple motions associated with membrane interaction.
Portrayal of complex dynamic properties of sugarcane defensin 5 by NMR: multiple motions associated with membrane interaction.
Structure. 2011 Jan 12;19(1):26-36
Authors: de Paula VS, Razzera G, Barreto-Bergter E, Almeida FC, Valente AP
Defensins are essentially ancient natural antibiotics with potent activity extending from lower organisms to humans. Sd5 is a recently described antifungal defensin that appears to be the...
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04-19-2011 11:01 PM
Solid-state (55)Mn NMR spectroscopy of bis(?-oxo)dimanganese(IV) [Mn(2)O(2)(salpn)(2)], a model for the oxygen evolving complex in photosystem II.
Solid-state (55)Mn NMR spectroscopy of bis(?-oxo)dimanganese(IV) , a model for the oxygen evolving complex in photosystem II.
Solid-state (55)Mn NMR spectroscopy of bis(?-oxo)dimanganese(IV) , a model for the oxygen evolving complex in photosystem II.
J Am Chem Soc. 2010 Dec 1;132(47):16727-9
Authors: Ellis PD, Sears JA, Yang P, Dupuis M, Boron TT, Pecoraro VL, Stich TA, Britt RD, Lipton AS
We have examined the antiferromagneticly coupled bis(?-oxo)dimanganese(IV) complex (1) with (55)Mn solid-state NMR at cryogenic temperatures and...
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03-13-2011 04:01 AM
[NMR paper] NMR studies of CCK-8/CCK1 complex support membrane-associated pathway for ligand-rece
NMR studies of CCK-8/CCK1 complex support membrane-associated pathway for ligand-receptor interaction.
Related Articles NMR studies of CCK-8/CCK1 complex support membrane-associated pathway for ligand-receptor interaction.
Can J Physiol Pharmacol. 2002 May;80(5):383-7
Authors: Giragossian C, Pellegrini M, Mierke DF
The interaction of peptide ligands with their associated G-protein-coupled receptors has been examined by a number of different experimental approaches over the years. We have been developing an approach utilizing high-resolution...
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11-24-2010 08:49 PM
[NMR paper] Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colic
Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain.
Related Articles Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain.
Biochemistry. 2001 Jun 26;40(25):7662-74
Authors: Huster D, Xiao L, Hong M
Solid-state NMR spectroscopy was employed to study the molecular dynamics of the colicin Ia channel domain in the soluble and membrane-bound states. In the soluble state, the protein executes small-amplitude librations (with...
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11-19-2010 08:32 PM
[NMR paper] The origin of differences in the physical properties of the equilibrium forms of cyto
The origin of differences in the physical properties of the equilibrium forms of cytochrome b5 revealed through high-resolution NMR structures and backbone dynamic analyses.
Related Articles The origin of differences in the physical properties of the equilibrium forms of cytochrome b5 revealed through high-resolution NMR structures and backbone dynamic analyses.
Biochemistry. 1998 Jun 9;37(23):8289-302
Authors: Dangi B, Sarma S, Yan C, Banville DL, Guiles RD
On the basis of a comparison of high-resolution solution structures calculated for...
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11-17-2010 11:06 PM
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy
Abstract Many biomolecular interactions proceed via a short-lived encounter state, consisting of multiple, lowly-populated species invisible to most experimental techniques. Recent development of paramagnetic relaxation enhancement (PRE) nuclear magnetic resonance (NMR) spectroscopy has allowed to directly visualize such transient intermediates in a number of protein-protein and protein-DNA complexes. Here we present an analysis of the recently published PRE NMR data for a protein complex of yeast...
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11-06-2010 01:24 PM
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy.
J Biomol NMR. 2010 Nov 4;
Authors: Volkov AN, Ubbink M, van Nuland NA
Many biomolecular interactions proceed via a short-lived encounter state, consisting of multiple, lowly-populated species invisible to most experimental techniques. Recent development of paramagnetic relaxation enhancement (PRE) nuclear magnetic resonance (NMR) spectroscopy has allowed to directly visualize such...
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11-05-2010 10:01 AM
[NMR paper] Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis
Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Complex of plastocyanin and cytochrome c characterized by NMR chemical shift analysis.
Biochemistry. 1997 May 27;36(21):6326-35
Authors: Ubbink M, Bendall DS
The complexes of horse ferrous and ferric cytochrome c with Cd-substituted pea plastocyanin have been characterized by nuclear magnetic resonance, in order to determine the binding sites and to study...
NMR analysis of the transient complex between membrane photosystem I and soluble cyto
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