Spectroscopic solution: NMR accesses membrane protein structures
Spectroscopic solution: NMR accesses membrane protein structures
Membrane proteins mediate so much of the information flow between cells and their surroundings. Understanding their molecular structure will inevitably give scientists insights into function and form as well as providing targets for novel pharmaceuticals when these proteins go awry.
Source: Spectroscopynow.com
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10-03-2011 08:40 PM
A solution NMR view of protein dynamics in the biological membrane.
A solution NMR view of protein dynamics in the biological membrane.
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...
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08-03-2011 12:00 PM
[NMR paper] Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
Related Articles Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR.
J Am Chem Soc. 2005 Sep 7;127(35):12263-72
Authors: Vogel A, Katzka CP, Waldmann H, Arnold K, Brown MF, Huster D
The human N-ras protein binds to cellular membranes by insertion of two covalently bound posttranslational lipid modifications, which is crucial for its...
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12-01-2010 06:56 PM
[NMR paper] Solution structure and dynamics of integral membrane proteins by NMR: a case study in
Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Related Articles Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Methods Enzymol. 2005;394:335-50
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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11-24-2010 11:14 PM
[NMR paper] NMR structure of Mistic, a membrane-integrating protein for membrane protein expressi
NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.
Related Articles NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.
Science. 2005 Feb 25;307(5713):1317-21
Authors: Roosild TP, Greenwald J, Vega M, Castronovo S, Riek R, Choe S
Although structure determination of soluble proteins has become routine, our understanding of membrane proteins has been limited by experimental bottlenecks in obtaining both sufficient yields of protein and ordered crystals. Mistic is an...
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11-24-2010 11:14 PM
[NMR paper] NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of
NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein.
Related Articles NMR solution structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein.
Biochemistry. 2004 Nov 30;43(47):14940-7
Authors: Biverståhl H, Andersson A, Gräslund A, Mäler L
The structure and membrane interaction of the N-terminal sequence (1-30) of the bovine prion protein (bPrPp) has been investigated by NMR spectroscopy in phospholipid membrane mimetic systems. CD spectroscopy...
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11-24-2010 10:03 PM
[NMR paper] NMR solution structure determination of membrane proteins reconstituted in detergent
NMR solution structure determination of membrane proteins reconstituted in detergent micelles.
Related Articles NMR solution structure determination of membrane proteins reconstituted in detergent micelles.
FEBS Lett. 2003 Nov 27;555(1):144-50
Authors: Fernández C, Wüthrich K
As an alternative to X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy in solution can be used for three-dimensional structure determination of small membrane proteins, preferably proteins with beta-barrel fold. This paper reviews recent achievements as...
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11-24-2010 09:16 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...