Abstract
This chapter describes an approach using designed proteins to understand the structure, spectroscopy, and dynamics of proteins that bind Cd(II). We will show that three-stranded coiled coils (3SCCs) based on the parent peptides TRI (Ac-G(LKALEEK)4G-NH2) or GRAND (Ac-G(LKALEEK)5G-NH2) have been essential for understanding how Cd(II) binds to thiolate-rich environments in proteins. Examples are given correlating physical properties such as the binding constants or deprotonation constants relating to structure. We present a scale that relates 113Cd NMR chemical shifts to structures extracted from 111mCd PAC experiments. In addition, we describe motional processes that help transport from the helical interface of proteins into the hydrophobic interior of helical bundles. These studies help clarify the chemistry of Cd(II) in relation to metal-regulated gene expression and detoxification.
An erratum to this chapter can be found at http://dx.doi.org/10.1007/978-94-007-5179-8_17
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Abbreviations
- &:
-
For the definition of the peptides see Table 1.
- Ala:
-
alanine
- ALAD:
-
aminolevulinic acid dehydratase
- Asp:
-
aspartic acid
- CD:
-
circular dichroism
- Cys:
-
cysteine
- EXAFS:
-
extended X-ray absorption fine structure
- Glu:
-
glutamic acid
- Gly:
-
glycine
- His:
-
histidine
- Hfl:
-
hexafluoroleucine
- Ile:
-
isoleucine
- Leu:
-
leucine
- LMCT:
-
ligand-to-metal charge-transfer
- Met:
-
methionine
- NOESY:
-
nuclear Overhauser effect specroscpy
- PAC:
-
perturbed angular correlation
- PDB:
-
Protein Data Bank
- Pen:
-
penicillamine
- NMR:
-
nuclear magnetic resonance
- 3SCC:
-
three-stranded coiled coil
- Ser:
-
serine
- Val:
-
valine
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Acknowledgments
A.F.A.P. thanks the University of Birmingham and V.L.P. thanks the University of Michigan and the National Institute of Health for support of this research (R01 ES0 12236).
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Peacock, A.F.A., Pecoraro, V.L. (2013). Natural and Artificial Proteins Containing Cadmium. In: Sigel, A., Sigel, H., Sigel, R. (eds) Cadmium: From Toxicity to Essentiality. Metal Ions in Life Sciences, vol 11. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5179-8_10
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