Amide proton exchange in human metallothionein-2 measured by nuclear magnetic resonance spectroscopy.
In human metallothionein-2, the exchange rate constants of ten amide protons were found to range from 1.7 x 10(-4) to 1 x 10(-1) min-1 at pH 6.3 and 8 degrees C. Most of these slowly exchanging protons could be associated with hydrogen bonds in secondary structure elements of the alpha-domain. Amide proton exchange rates thus present an additional criterion for the structural characterization of different metallothioneins, which could be particularly valuable for comparisons of different homologous protein preparations containing nuclear magnetic resonance-inactive metal ions, where the metal-polypeptide co-ordinative bonds cannot be identified directly.
Messerle
B A
BA
Institut für Molecularbiologie un Biophysik, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
Bos
M
M
Schäffer
A
A
Vasák
M
M
Kägi
J H
JH
Wüthrich
K
K
D000577:Amides; D000595:Amino Acid Sequence; D006801:Humans; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008668:Metallothionein; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011522:Protons
D000577:Amides; D011522:Protons; D008668:Metallothionein