Related ArticlesTwo-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 two-dimensional NMR techniques. Of 62 amino acid residues in cobrotoxin, the complete assignments of 58 residues have been made. The resonances from several of the remaining residues have been identified but not yet specifically assigned. The secondary structure of an antiparallel triple- and double-stranded beta-sheet has also been determined by observing the NOE.
[NMR paper] Studies on solution NMR structure of brazzein : Secondary structure and molecular sca
Studies on solution NMR structure of brazzein : Secondary structure and molecular scaffold.
Related Articles Studies on solution NMR structure of brazzein : Secondary structure and molecular scaffold.
Sci China C Life Sci. 1999 Aug;42(4):409-19
Authors: Gao G, Dai J, Ding M, Hellekant G, Wang J, Wang D
Brazzein is a sweet-tasting protein isolated from the fruit of West African plantPentadiplandra brazzeana Baillon. It is the smallest and the most water-soluble sweet protein discovered so far and is highly thermostable. The proton NMR study of...
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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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[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 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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[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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[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] The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
The NMR structure of cyclosporin A bound to cyclophilin in aqueous solution.
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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....