Abstract
Previous studies showed that metals in the β-domain of metallothionein (MT) are more readily exchangeable and the level of avidity is site specific. This is reflected by energy differences computed with a series of simulated structures derived from X-ray crystallography. In this study, we examined further the contribution of each of the nine cysteines in the β-domain. By semi-empirical MNDO calculations, we observed that the relative average binding strength is the strongest for Cys21 to Cd[M4] and for Cys26 to Zn[M3], except for the bridging cysteines. These results suggest that binding site preference for Zn/Cd is determined by binding strength between specific cysteines and metal ion species.
Original language | English (US) |
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Pages (from-to) | 41-46 |
Number of pages | 6 |
Journal | Protein engineering |
Volume | 11 |
Issue number | 1 |
State | Published - Jan 1998 |
Externally published | Yes |
Keywords
- Binding energy
- MNDO
- Metallothionein
- Quantum
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology