Related ArticlesNMR studies of lantibiotics. The structure of nisin in aqueous solution.
Eur J Biochem. 1991 Dec 18;202(3):1181-8
Authors: Van de Ven FJ, Van den Hooven HW, Konings RN, Hilbers CW
Nisin is a posttranslationally modified protein of 34 amino acids, and is a member of the class of bacteriocidal polypeptides known as lantibiotics, that contain the unusual amino acid lanthionine. Its structure in aqueous solution has been determined on the basis of NMR data, i.e. interproton distance constraints derived from nuclear Overhauser enhancement spectroscopy and torsion angle constraints derived from double-quantum-filtered correlated spectroscopy. Translation of the NMR constraints into a three-dimensional structure was carried out with the distance-geometry program DISMAN, followed by restrained energy minimization using CHARMm. The internal mobility of the peptide chain prohibited the determination of a precise overall folding of the molecule, but parts of the structure could be obtained, albeit sometimes with low resolution. The structure of nisin can best be defined as follows. The outermost N-terminal and C-terminal regions of nisin appear quite flexible, the remainder of the molecule consists of an amphiphilic N-terminal fragment (residues 3-19), joined by a flexible 'hinge' region to a rigid double-ring fragment formed by residues 23-28. The latter fragment has the appearance of a somewhat overwound alpha-helix. It is suggested, by assuming the presence of a (transient) alpha-helical structure in this part of prenisin, that the coupling between residues 23 and 26, as well as between 25 and 28, by thioether bridges, and the inversion of the C alpha chiralities at positions 23 and 25, can be rationalized.
[NMR paper] NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing co
NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
Biochemistry. 1997 Apr 1;36(13):3959-70
Authors: Zhang O, Forman-Kay JD
The isolated N-terminal SH3 domain of the Drosophila adapter protein drk (drkN SH3 domain) exists in a dynamic equilibrium between a folded (F(exch)) and an unfolded (U(exch)) state...
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[NMR paper] NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing co
NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
Biochemistry. 1997 Apr 1;36(13):3959-70
Authors: Zhang O, Forman-Kay JD
The isolated N-terminal SH3 domain of the Drosophila adapter protein drk (drkN SH3 domain) exists in a dynamic equilibrium between a folded (F(exch)) and an unfolded (U(exch)) state...
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08-22-2010 03:03 PM
[NMR paper] NMR studies of lantibiotics. The structure of nisin in aqueous solution.
NMR studies of lantibiotics. The structure of nisin in aqueous solution.
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 NMR studies of lantibiotics. The structure of nisin in aqueous solution.
Eur J Biochem. 1991 Dec 18;202(3):1181-8
Authors: Van de Ven FJ, Van den Hooven HW, Konings RN, Hilbers CW
Nisin is a posttranslationally modified protein of 34 amino acids, and is a member of the class of bacteriocidal polypeptides known...
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08-21-2010 11:12 PM
[NMR paper] 3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to
3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to tertiary structure determination from a small basis of 1H NMR NOE correlations.
Related Articles 3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to tertiary structure determination from a small basis of 1H NMR NOE correlations.
J Biomol NMR. 1991 Sep;1(3):283-98
Authors: Rico M, Santoro J, González C, Bruix M, Neira JL, Nieto JL, Herranz J
A method is proposed to generate initial structures in cases where the distance...
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[NMR paper] 3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to
3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to tertiary structure determination from a small basis of 1H NMR NOE correlations.
Related Articles 3D structure of bovine pancreatic ribonuclease A in aqueous solution: an approach to tertiary structure determination from a small basis of 1H NMR NOE correlations.
J Biomol NMR. 1991 Sep;1(3):283-98
Authors: Rico M, Santoro J, González C, Bruix M, Neira JL, Nieto JL, Herranz J
A method is proposed to generate initial structures in cases where the distance...
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08-21-2010 11:12 PM
[NMR paper] The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
Related Articles The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
Biochemistry. 1991 Jul 2;30(26):6563-74
Authors: Weber C, Wider G, von Freyberg B, Traber R, Braun W, Widmer H, Wüthrich K
Cyclosporin A bound to the presumed receptor protein cyclophilin was studied in aqueous solution at pH 6.0 by nuclear magnetic resonance spectroscopy using uniform 15N- or 13C-labeling of cyclosporin A and heteronuclear spectral editing techniques....
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[NMR paper] The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
Related Articles The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
Biochemistry. 1991 Jul 2;30(26):6563-74
Authors: Weber C, Wider G, von Freyberg B, Traber R, Braun W, Widmer H, Wüthrich K
Cyclosporin A bound to the presumed receptor protein cyclophilin was studied in aqueous solution at pH 6.0 by nuclear magnetic resonance spectroscopy using uniform 15N- or 13C-labeling of cyclosporin A and heteronuclear spectral editing techniques....
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08-21-2010 11:12 PM
[NMR paper] Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution
Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution.
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 Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution.
Eur J Biochem. 1990 Nov 13;193(3):789-99
Authors: Yu C, Lee CS, Chuang LC, Shei YR, Wang CY
The 1H-NMR spectra of cobrotoxin, a neurotoxic protein isolated from Formosan cobra Naja naja atra, have been studied by...