Related ArticlesHigh-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium.
J Biomol NMR. 1997 Oct;10(3):289-92
Authors: Bax A, Tjandra N
A mixture of dihexanoyl phosphatidylcholine and dimyristoyl phosphatidylcholine in water forms disc-shaped particles, often referred to as bicelles [Sanders and Schwonek (1992) Biochemistry, 31, 8898-8905]. These adopt an ordered, liquid crystalline phase, which can be maintained at very low concentrations of the bicelles (down to 3% w/v). At this concentration the spacing between individual bicelles, on average, exceeds 300 A. The bicelles are shown to have a negligible effect on the rotational diffusion of ubiquitin as judged by the 15N T1p values of the backbone amides relative to those in isotropic aqueous solution. The protein exhibits a residual degree of alignment which is proportional to the bicelle concentration, and approximately collinear with ubiquitin's rotational diffusion tensor. The degree of alignment obtained offers unique opportunities for studying the protein's structure and dynamics.
[NMR paper] High-resolution solid-state NMR studies on uniformly [13C,15N]-labeled ubiquitin.
High-resolution solid-state NMR studies on uniformly -labeled ubiquitin.
Related Articles High-resolution solid-state NMR studies on uniformly -labeled ubiquitin.
Chembiochem. 2005 Sep;6(9):1638-47
Authors: Seidel K, Etzkorn M, Heise H, Becker S, Baldus M
Understanding of the effects of intermolecular interactions, molecular dynamics, and sample preparation on high-resolution magic-angle spinning NMR data is currently limited. Using the example of a uniformly -labeled sample of ubiquitin, we discuss solid-state NMR methods tailored to the...
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[NMR paper] High-resolution NMR studies of encapsulated proteins in liquid ethane.
High-resolution NMR studies of encapsulated proteins in liquid ethane.
High-resolution NMR studies of encapsulated proteins in liquid ethane.
J Am Chem Soc. 2005 Jul 27;127(29):10176-7
Authors: Peterson RW, Lefebvre BG, Wand AJ
Many of the difficulties presented by large, aggregation-prone, and membrane proteins to modern solution NMR spectroscopy can be alleviated by actively seeking to increase the effective rate of molecular reorientation. An emerging approach involves encapsulating the protein of interest within the protective shell of a...
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[NMR paper] High-resolution solution NMR structure of the minimal active domain of the human immu
High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Related Articles High-resolution solution NMR structure of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.
Biochemistry. 1998 Dec 22;37(51):17704-13
Authors: Kodera Y, Sato K, Tsukahara T, Komatsu H, Maeda T, Kohno T
The retroviral nucleocapsid (NC) protein is a multifunctional protein essential for RNA genome packaging and viral infectivity. The NC protein, NCp8, of the...
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[NMR paper] High-resolution solution structure of the inhibitor-free catalytic fragment of human
High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.
Related Articles High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.
Biochemistry. 1998 Feb 10;37(6):1495-504
Authors: Moy FJ, Chanda PK, Cosmi S, Pisano MR, Urbano C, Wilhelm J, Powers R
The high-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase (MMP-1), a...
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[NMR paper] The three-dimensional high resolution structure of human interferon alpha-2a determin
The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.
J Mol Biol. 1997 Dec 12;274(4):661-75
Authors: Klaus W, Gsell B, Labhardt AM, Wipf B, Senn H
The solution structure of recombinant human interferon...
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[NMR paper] A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c
A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex.
Eur J Biochem. 1992 Sep 15;208(3):713-20
Authors: Tuzi S,...
High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline
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