Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.
Braun, W, Vasák, M, Robbins, A H, Stout, C D, Wagner, G, Kägi, J H, ...
Metallothioneins are small cysteine-rich proteins capable of binding heavy metal ions such as Zn2+ and Cd2+. They are ubiquitous tissue components in higher organisms, which tentatively have been...
Metal thiolate clusters in cobalt(II)-metallothionein.
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...
Abrahams, I L, Bremner, I, Diakun, G P, Garner, C D, Hasnain, S S, Ross, I, ...
Zn-metallothionein 1 from rabbit liver was investigated by means of Zn K-edge extended X-ray-absorption fine structure (e.x.a.f.s.). Also, the Cu and Zn K-edge e.x.a.f.s. were measured for two...
Rabbit 113Cd7-metallothionein-2a (MT) contains two metal-thiolate clusters of three (cluster B) and four (cluster A) metal ions. The 113Cd-n.m.r. spectrum of 113Cd6-MT, isolated from 113Cd7-MT upon...
Dynamic metal-thiolate cluster structure of metallothioneins.
113Cd-NMR studies have established that vertebrate and invertebrate metallothioneins contain two unique metal-thiolate clusters. However, it proved to be difficult to account theoretically for all...
Structure of mammalian metallothionein.
Kägi, J H, Vasák, M, Lerch, K, Gilg, D E, Hunziker, P, Bernhard, W R, ...
All mammalian metallothioneins characterized contain a single polypeptide chain of 61 amino acid residues, among them 20 cysteines providing the ligands for seven metal-binding sites. Native...
Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.
Braun, W, Vasák, M, Robbins, A H, Stout, C D, Wagner, G, Kägi, J H, ...
Metallothioneins are small cysteine-rich proteins capable of binding heavy metal ions such as Zn2+ and Cd2+. They are ubiquitous tissue components in higher organisms, which tentatively have been...
Metal thiolate clusters in cobalt(II)-metallothionein.
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...
Abrahams, I L, Bremner, I, Diakun, G P, Garner, C D, Hasnain, S S, Ross, I, ...
Zn-metallothionein 1 from rabbit liver was investigated by means of Zn K-edge extended X-ray-absorption fine structure (e.x.a.f.s.). Also, the Cu and Zn K-edge e.x.a.f.s. were measured for two...
Rabbit 113Cd7-metallothionein-2a (MT) contains two metal-thiolate clusters of three (cluster B) and four (cluster A) metal ions. The 113Cd-n.m.r. spectrum of 113Cd6-MT, isolated from 113Cd7-MT upon...
Dynamic metal-thiolate cluster structure of metallothioneins.
113Cd-NMR studies have established that vertebrate and invertebrate metallothioneins contain two unique metal-thiolate clusters. However, it proved to be difficult to account theoretically for all...
Structure of mammalian metallothionein.
Kägi, J H, Vasák, M, Lerch, K, Gilg, D E, Hunziker, P, Bernhard, W R, ...
All mammalian metallothioneins characterized contain a single polypeptide chain of 61 amino acid residues, among them 20 cysteines providing the ligands for seven metal-binding sites. Native...
Henehan, C. J., Pountney, D. L., Zerbe, O., Vasák, M.
Optical and NMR methods are presented for the identification of cysteine ligands in Cd-substituted metalloproteins, in particular those containing zinc-fingerlike motifs, using Cd-substituted...
Pountney, D. L., Henehan, C. J., Vasák, M.
Far-UV CD, 1H-NMR, and Fourier transform infrared (FTIR) spectroscopy are three of the most commonly used methods for the determination of protein secondary structure composition. These methods are...