A solution NMR view of protein dynamics in the biological membrane.
Curr Opin Struct Biol. 2011 Jul 30;
Authors: Chill JH, Naider F
Structure determination of membrane-associated proteins (MPs) represents a frontier of structural biology that is characterized by unique challenges in sample preparation and data acquisition. No less important is our ability to study the dynamics of MPs, since MP flexibility and characteristic motions often make sizeable contributions to their function. This review focuses on solution state NMR methods to characterize dynamics of MPs in the membrane environment. NMR approaches to study molecular motions on a wide range of time-scales and their application to membrane proteins are described. Studies of polytopic and bitopic MPs demonstrating the power of such methods to characterize the dynamic behavior of MPs and their interaction with the membrane-mimicking surroundings are presented. Attempts are made to place the dynamic conclusions into a biological context. The importance and limitations of such investigations guarantee that further developments in this field will be actively pursued.
PMID: 21807499 [PubMed - as supplied by publisher]
Protein dynamics and allostery: an NMR view.
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Curr Opin Struct Biol. 2010 Nov 23;
Authors: Tzeng SR, Kalodimos CG
Allostery, the process by which distant sites within a protein system are energetically coupled, is an efficient and ubiquitous mechanism for activity regulation. A purely mechanical view of allostery invoking only structural changes has developed over the decades as the classical view of the phenomenon. However, a fast growing list of examples illustrate the intimate link...
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11-27-2010 02:45 PM
[NMR paper] Solution structure and dynamics of integral membrane proteins by NMR: a case study in
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Authors: Hwang PM, Kay LE
Solution NMR spectroscopy is rapidly becoming an important technique for the study of membrane protein structure and dynamics. NMR experiments on large perdeuterated proteins typically exploit the favorable relaxation properties of backbone amide...
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[NMR paper] Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative
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J Lipid Res. 2002 Jan;43(1):132-40
Authors: Corcelli A, Lattanzio VM, Mascolo G, Papadia P, Fanizzi F
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11-24-2010 08:49 PM
[NMR paper] Biological membrane structure by solid-state NMR.
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Authors: Auger M
Nuclear magnetic resonance (NMR) spectroscopy, and particularly solid-state NMR spectroscopy, is a method of choice to study the structure and dynamics of both the lipid and the protein components of model and biological membranes. Different approaches have been developed to study these systems in which the restricted molecular motions result in broad NMR spectra. This...
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11-19-2010 08:29 PM
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Biochim Biophys Acta. 2010 Aug 18;
Authors: Cook GA, Opella SJ
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08-25-2010 02:04 PM
Simultaneous Structure and Dynamics of a Membrane Protein using REDCRAFT: Membrane-bo
Simultaneous Structure and Dynamics of a Membrane Protein using REDCRAFT: Membrane-bound form of Pf1 Coat Protein
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 30 July 2010</br>
Paul, Shealy , Mikhail, Simin , Sang Ho, Park , Stanley J., Opella , Homayoun, Valafar</br>
A strategy for simultaneous study of the structure and internal dynamics of a membrane protein is described using the REDCRAFT algorithm. The membrane-bound form of the Pf1 major coat protein (mbPf1) was used as an example. First, synthetic data is...
A solution NMR view of protein dynamics in the biological membrane.
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