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Cadmium: From Toxicity to Essentiality

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Attention for Chapter 10: Natural and Artificial Proteins Containing Cadmium
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Chapter title
Natural and Artificial Proteins Containing Cadmium
Chapter number 10
Book title
Cadmium: From Toxicity to Essentiality
Published in
Metal ions in life sciences, February 2016
DOI 10.1007/978-94-007-5179-8_10
Pubmed ID
Book ISBNs
978-9-40-075178-1, 978-9-40-075179-8

Anna F. A. Peacock, Vincent L. Pecoraro


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)(4)G-NH(2)) or GRAND (Ac-G(LKALEEK)(5)G-NH(2)) 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 (113)Cd NMR chemical shifts to structures extracted from (111m)Cd 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.

Mendeley readers

The data shown below were compiled from readership statistics for 11 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 11 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 3 27%
Student > Ph. D. Student 3 27%
Professor 1 9%
Student > Bachelor 1 9%
Other 1 9%
Other 0 0%
Unknown 2 18%
Readers by discipline Count As %
Chemistry 5 45%
Agricultural and Biological Sciences 3 27%
Biochemistry, Genetics and Molecular Biology 1 9%
Unknown 2 18%