| 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
|
| Authors |
Anna F. A. Peacock, Vincent L. Pecoraro |
| 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)(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
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 13 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 4 | 31% |
| Student > Ph. D. Student | 3 | 23% |
| Professor | 1 | 8% |
| Other | 1 | 8% |
| Student > Master | 1 | 8% |
| Other | 1 | 8% |
| Unknown | 2 | 15% |
| Readers by discipline | Count | As % |
|---|---|---|
| Chemistry | 5 | 38% |
| Agricultural and Biological Sciences | 3 | 23% |
| Biochemistry, Genetics and Molecular Biology | 3 | 23% |
| Unknown | 2 | 15% |