Related ArticlesClose encounters of the transient kind: protein interactions in the photosynthetic redox chain investigated by NMR spectroscopy.
Acc Chem Res. 2003 Oct;36(10):723-30
Authors: Crowley PB, Ubbink M
Plastocyanin and cytochrome c(6) function as electron shuttles between cytochrome f and photosystem I in the photosynthetic redox chain. To transfer electrons the partners form transient complexes, which are remarkably short-lived (milliseconds or less). Recent nuclear magnetic resonance studies have revealed details of the molecular interfaces found in such complexes. General features include a small binding site with a hydrophobic core and a polar periphery, including some charged residues. Furthermore, it was found that the interactions are relatively nonspecific. The structural information, in combination with kinetic and theoretical analyses of protein complexes, provides new insight into the nature of transient protein interactions.
Up Close with Membrane Lipid-Protein Complexes - Science Careers Blog (subscription)
Up Close with Membrane Lipid-Protein Complexes - Science Careers Blog (subscription)
<img alt="" height="1" width="1" />
Up Close with Membrane Lipid-Protein Complexes
Science Careers Blog (subscription)
(2) report mass spectrometry of intact integral membrane protein complexes solubilized from bilayers. The results show that specific structural lipids remain bound in the gas phase and can be counted. Despite some technical hurdles, integral membrane ...
Read here
nmrlearner
Online News
0
10-21-2011 09:52 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these interactions...
nmrlearner
Journal club
0
09-30-2011 06:00 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these...
nmrlearner
Journal club
0
09-30-2011 05:59 AM
[Question from NMRWiki Q&A forum] Error 113: lid is close
Error 113: lid is close
Was trying to lift sample in BMSB control suite... but the machine detected sample within and an error 113 popped out. Anyone knows how to solve this? Thanks in advance.
Check if somebody has answered this question on NMRWiki QA forum
nmrlearner
News from other NMR forums
0
04-12-2011 01:10 PM
[NMR paper] Probing the kinetic landscape of transient peptide-protein interactions by use of pep
Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
Related Articles Probing the kinetic landscape of transient peptide-protein interactions by use of peptide (15)n NMR relaxation dispersion spectroscopy: binding of an antithrombin peptide to human prothrombin.
J Am Chem Soc. 2003 Oct 15;125(41):12432-42
Authors: Tolkatchev D, Xu P, Ni F
Protein-ligand interactions may lead to the formation of multiple...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C
Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.
Related Articles Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin.
Biochemistry. 2003 Jun 17;42(23):7068-76
Authors: Worrall JA, Reinle W, Bernhardt R, Ubbink M
The interaction between yeast iso-1-cytochrome c (C102T) and two forms of bovine adrenodoxin, the wild type and a truncated form comprising residues 4-108, has been investigated using a combination of one- and two-dimensional...
nmrlearner
Journal club
0
11-24-2010 09:01 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...
nmrlearner
Journal club
0
11-05-2010 10:01 AM
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution - Sec
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution - Securities Industry News (blog) (subscription)
<img alt="" height="1" width="1" />
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution
Securities Industry News (blog) (subscription)
In this work, we used chemical shifts and bond-vector orientation constraints obtained from nuclear magnetic resonance relaxation dispersion spectroscopy, ...
Read More
Close encounters of the transient kind: protein interactions in the photosynthetic re
Linear Mode
