[NMR paper] Study of ion translocation by respiratory complex I. A new insight using (23)Na NMR spectroscopy.
Study of ion translocation by respiratory complex I. A new insight using (23)Na NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Study of ion translocation by respiratory complex I. A new insight using (23)Na NMR spectroscopy.
Biochim Biophys Acta. 2012 Oct;1817(10):1810-6
Authors: Batista AP, Marreiros BC, Louro RO, Pereira MM
Abstract
The research on complex I has gained recently a new enthusiasm, especially after the resolution...
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05-04-2013 09:18 PM
‘q-titration’ of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy
‘q-titration’ of long-chain and short-chain lipids differentiates between structured and mobile residues of membrane proteins studied in bicelles by solution NMR spectroscopy
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 25 October 2011</br>
Woo Sung*Son, Sang Ho*Park, Henry J.*Nothnagel, George J.*Lu, Yan*Wang, ...</br>
‘q-titration’ refers to the systematic comparison of signal intensities in solution NMR spectra of uniformlyN labeled membrane proteins solubilized in micelles and isotropic bicelles as a function of the molar ratios (q) of the...
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10-26-2011 11:25 AM
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Threonine side chain conformational population distribution of a type I antifreeze protein on interacting with ice surface studied via (13)C-(15)N dynamic REDOR NMR.
Solid State Nucl Magn Reson. 2011 Mar 23;
Authors: Mao Y, Jeong M, Wang T, Ba Y
Antifreeze proteins (AFPs) provide survival mechanism for species living in subzero environments by lowering the freezing points of their...
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04-08-2011 10:00 AM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 27;
Authors: Esadze A, Li DW, Wang T, Bru?schweiler R, Iwahara J
Despite their importance in macromolecular interactions and functions, the dynamics of lysine side-chain amino groups in proteins are not well understood. In this study, we have developed the methodology for the investigations of the dynamics...
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12-29-2010 04:04 PM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Alexandre Esadze, Da-Wei Li, Tianzhi Wang, Rafael Bru?schweiler and Junji Iwahara
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107847d/aop/images/medium/ja-2010-07847d_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107847d
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/iFwgRBt-zto
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12-28-2010 05:27 AM
[NMR paper] Millisecond protein folding studied by NMR spectroscopy.
Millisecond protein folding studied by NMR spectroscopy.
Related Articles Millisecond protein folding studied by NMR spectroscopy.
Protein Pept Lett. 2005 Feb;12(2):139-46
Authors: Zeeb M, Balbach J
Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond...
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11-24-2010 11:14 PM
[NMR paper] Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR an
Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
Related Articles Prion protein interaction with the C-terminal SH3 domain of Grb2 studied using NMR and optical spectroscopy.
Biochemistry. 2004 Aug 17;43(32):10393-9
Authors: Lysek DA, Wüthrich K
Transmissible spongiform encephalopathies have been observed exclusively in organisms expressing the host-encoded prion protein (PrP). The function of the cellular isoform of PrP found in healthy organisms has so far not been identified,...
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11-24-2010 10:01 PM
[NMR paper] Protein complexes studied by NMR spectroscopy.
Protein complexes studied by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein complexes studied by NMR spectroscopy.
Curr Opin Biotechnol. 1996 Aug;7(4):403-8
Authors: Wand AJ, Englander SW
Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point...
Protein–protein interaction in Rhodothermus marinus respiratory chain studied by NMR spectroscopy
Linear Mode
