Vasák M - Search Results

1

Solution structure of native proteins with irregular folds from Raman optical activity.

Smyth E, Syme CD, Blanch EW, Hecht L, Vasák M, Barron LD. Smyth E, et al. Among authors: vasak m. Biopolymers. 2001 Feb;58(2):138-51. doi: 10.1002/1097-0282(200102)58:2<138::AID-BIP30>3.0.CO;2-W. Biopolymers. 2001. PMID: 11093113

2

Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution.

Braun W, Wagner G, Wörgötter E, Vasák M, Kägi JH, Wüthrich K. Braun W, et al. Among authors: vasak m. J Mol Biol. 1986 Jan 5;187(1):125-9. doi: 10.1016/0022-2836(86)90412-2. J Mol Biol. 1986. PMID: 3959078

3

Nuclear magnetic resonance identification of "half-turn" and 3(10)-helix secondary structure in rabbit liver metallothionein-2.

Wagner G, Neuhaus D, Wörgötter E, Vasák M, Kägi JH, Wüthrich K. Wagner G, et al. Among authors: vasak m. J Mol Biol. 1986 Jan 5;187(1):131-5. doi: 10.1016/0022-2836(86)90413-4. J Mol Biol. 1986. PMID: 3959079

4

Spatial structure of rabbit liver metallothionein-2 in solution by NMR.

Wagner G, Frey MH, Neuhaus D, Wörgötter E, Braun W, Vasak M, Kägi JH, Wüthrich K. Wagner G, et al. Among authors: vasak m. Experientia Suppl. 1987;52:149-57. doi: 10.1007/978-3-0348-6784-9_8. Experientia Suppl. 1987. PMID: 2959501

5

Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy.

Messerle BA, Schäffer A, Vasák M, Kägi JH, Wüthrich K. Messerle BA, et al. Among authors: vasak m. J Mol Biol. 1992 May 20;225(2):433-43. doi: 10.1016/0022-2836(92)90930-i. J Mol Biol. 1992. PMID: 1593628

6

Amide proton exchange in human metallothionein-2 measured by nuclear magnetic resonance spectroscopy.

Messerle BA, Bos M, Schäffer A, Vasák M, Kägi JH, Wüthrich K. Messerle BA, et al. Among authors: vasak m. J Mol Biol. 1990 Aug 5;214(3):781-6. doi: 10.1016/0022-2836(90)90292-T. J Mol Biol. 1990. PMID: 2167380

7

Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy.

Messerle BA, Schäffer A, Vasák M, Kägi JH, Wüthrich K. Messerle BA, et al. Among authors: vasak m. J Mol Biol. 1990 Aug 5;214(3):765-79. doi: 10.1016/0022-2836(90)90291-S. J Mol Biol. 1990. PMID: 2388267

8

Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy.

Schultze P, Wörgötter E, Braun W, Wagner G, Vasák M, Kägi JH, Wüthrich K. Schultze P, et al. Among authors: vasak m. J Mol Biol. 1988 Sep 5;203(1):251-68. doi: 10.1016/0022-2836(88)90106-4. J Mol Biol. 1988. PMID: 3184190

9

Metal co-ordination in rat liver metallothionein-2 prepared with or without reconstitution of the metal clusters, and comparison with rabbit liver metallothionein-2.

Vasák M, Wörgötter E, Wagner G, Kägi JH, Wüthrich K. Vasák M, et al. J Mol Biol. 1987 Aug 5;196(3):711-9. doi: 10.1016/0022-2836(87)90042-8. J Mol Biol. 1987. PMID: 3681973

10

Metal thiolate clusters in cobalt(II)-metallothionein.

Vasák M, Kägi JH. Vasák M, et al. Proc Natl Acad Sci U S A. 1981 Nov;78(11):6709-13. doi: 10.1073/pnas.78.11.6709. Proc Natl Acad Sci U S A. 1981. PMID: 6273885 Free PMC article.

Rabbit liver metallothionein-1 in which all seven metal-binding sites are occupied by cobalt(II) exhibits spectral features typical of tetrathiolate coordination with approximate Td microsymmetry [Vasak, M. (1980) J. Am. Chem. Soc. 102, 3953-3955]. With a total of 2 …

Rabbit liver metallothionein-1 in which all seven metal-binding sites are occupied by cobalt(II) exhibits spectral features typical of tetra …

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