Chapter

Cadmium: From Toxicity to Essentiality

Volume 11 of the series Metal Ions in Life Sciences pp 303-337

Date:

Natural and Artificial Proteins Containing Cadmium

  • Anna F. A. PeacockAffiliated withDepartment of Chemistry, University of Michigan Email author 
  • , Vincent L. PecoraroAffiliated withSchool of Chemistry, University of Birmingham Email author 

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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.

Keywords

coiled coil de novo design peptide protein thiol