Related ArticlesSequence-specific 1H-NMR assignments and folding topology of human CD59.
Protein Sci. 1993 Dec;2(12):2015-27
Authors: Fletcher CM, Harrison RA, Lachmann PJ, Neuhaus D
CD59 is a recently discovered cell-surface glycoprotein that restricts lysis by homologous complement and has limited sequence similarity to snake venom neurotoxins. This paper describes the first results of a two-dimensional NMR study of CD59 prepared from human urine. Nearly complete 1H-NMR assignments were obtained for the 77 amino acid residues and partial assignments for the N-glycan and the glycosylphosphatidylinositol (GPI) anchor. These results together confirm that the C-terminal residue of the mature protein is Asn 77 and that the urine-derived form retains the nonlipid part of the GPI anchor. The data further indicate that the GPI anchor and possibly the N-glycan are structurally inhomogeneous and suggest that the phospholipid present in the intact GPI anchor was removed by phosphatidylinositol-specific phospholipase-D. The folding topology of the protein was determined from NOE enhancements and slowly exchanging backbone amide protons and consists primarily of five extended strands (denoted beta 1-beta 5 in sequence order), arranged into separate two-stranded (beta 1 and beta 2) and three-stranded (beta 3-beta 5) antiparallel beta-sheets. The same folding topology is found in all of the snake venom neurotoxins whose structures have been determined. The region between the beta 4 and beta 5 strands has helical character, a feature that is not present in the neurotoxins but that is seen in the topologically similar wheat germ agglutinin.
[NMR paper] Sequence-specific 1H NMR resonance assignments and secondary structure of human apoli
Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Related Articles Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate.
Biochem Cell Biol. 1998;76(2-3):267-75
Authors: Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ
Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we...
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[NMR paper] Chemical shift assignments and folding topology of the Ras-binding domain of human Ra
Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1994 Jun 28;33(25):7745-52
Authors: Emerson SD, Waugh DS, Scheffler JE, Tsao KL, Prinzo KM, Fry DC
Raf-1 is a 74-kDa serine-threonine kinase which serves as the immediate downstream target of Ras in the...
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[NMR paper] Chemical shift assignments and folding topology of the Ras-binding domain of human Ra
Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Related Articles Chemical shift assignments and folding topology of the Ras-binding domain of human Raf-1 as determined by heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1994 Jun 28;33(25):7745-52
Authors: Emerson SD, Waugh DS, Scheffler JE, Tsao KL, Prinzo KM, Fry DC
Raf-1 is a 74-kDa serine-threonine kinase which serves as the immediate downstream target of Ras in the...
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[NMR paper] Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT
Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR.
Related Articles Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR.
Biochemistry. 1993 Dec 7;32(48):13071-80
Authors: Abeygunawardana C, Weber DJ, Frick DN, Bessman MJ, Mildvan AS
The MutT protein, a 129-residue enzyme from Escherichia coli which prevents A.T-->C.G mutations, catalyzes the hydrolysis of nucleoside triphosphates (NTP)...
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[NMR paper] Sequence-specific 1H NMR assignments and secondary structure of the streptococcal pro
Sequence-specific 1H NMR assignments and secondary structure of the streptococcal protein G B2-domain.
Related Articles Sequence-specific 1H NMR assignments and secondary structure of the streptococcal protein G B2-domain.
Biochemistry. 1992 Apr 14;31(14):3604-11
Authors: Orban J, Alexander P, Bryan P
Two-dimensional NMR spectroscopy has been used to obtain sequence-specific 1H NMR assignments for the IgG-binding B2-domain of streptococcal protein G. Secondary structure elements were identified from analysis of characteristic backbone-backbone...
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[NMR paper] Sequence-specific NMR assignments of the trp repressor from Escherichia coli using th
Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
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 Sequence-specific NMR assignments of the trp repressor from Escherichia coli using three-dimensional 15N/1H heteronuclear techniques.
Eur J Biochem. 1992 Feb 15;204(1):137-46
Authors: Borden KL, Bauer CJ, Frenkiel TA, Beckmann P, Lane AN
...
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[NMR paper] Sequence-specific 1H NMR assignments and determination of the secondary structure for
Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B.
Related Articles Sequence-specific 1H NMR assignments and determination of the secondary structure for the activation domain isolated from pancreatic procarboxypeptidase B.
Biochemistry. 1990 Aug 14;29(32):7515-22
Authors: Vendrell J, Wider G, Avilés FX, Wüthrich K
Nearly complete sequence-specific 1H NMR assignments are presented for amino acid residues 3-81 in the 81-residue globular...
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[NMR paper] Complete sequence-specific 1H NMR assignments for human insulin.
Complete sequence-specific 1H NMR assignments for human insulin.
Related Articles Complete sequence-specific 1H NMR assignments for human insulin.
Biochemistry. 1990 Mar 27;29(12):2906-13
Authors: Kline AD, Justice RM
Solvent conditions where human insulin could be studied by high-resolution NMR were determined. Both low pH and addition of acetonitrile were required to overcome the protein's self-association and to obtain useful spectra. Two hundred eighty-six 1H resonances were located and assigned to specific sites on the protein by using...
Sequence-specific 1H-NMR assignments and folding topology of human CD59.
Linear Mode
