Supramolecular control of heme binding and electronic states in multi-heme peptide assemblies
Abstract
Three peptides that are compositionally identical but sequentially distinct have been designed to study the impact of morphology and hydrophobicity on heme coordination and function.
- Authors:
-
- Argonne National Lab. (ANL), Argonne, IL (United States). Center for Nanoscale Materials
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1393443
- Grant/Contract Number:
- AC02-06CH11357
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Organic and Biomolecular Chemistry
- Additional Journal Information:
- Journal Volume: 15; Journal Issue: 32; Journal ID: ISSN 1477-0520
- Publisher:
- Royal Society of Chemistry
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Peptide amphiphile; heme; supramolecular; self-assembly; biomolecular material
Citation Formats
Christopher Fry, H., Wood, Anna R., and Solomon, Lee A. Supramolecular control of heme binding and electronic states in multi-heme peptide assemblies. United States: N. p., 2017.
Web. doi:10.1039/c7ob01081h.
Christopher Fry, H., Wood, Anna R., & Solomon, Lee A. Supramolecular control of heme binding and electronic states in multi-heme peptide assemblies. United States. https://doi.org/10.1039/c7ob01081h
Christopher Fry, H., Wood, Anna R., and Solomon, Lee A. Sun .
"Supramolecular control of heme binding and electronic states in multi-heme peptide assemblies". United States. https://doi.org/10.1039/c7ob01081h. https://www.osti.gov/servlets/purl/1393443.
@article{osti_1393443,
title = {Supramolecular control of heme binding and electronic states in multi-heme peptide assemblies},
author = {Christopher Fry, H. and Wood, Anna R. and Solomon, Lee A.},
abstractNote = {Three peptides that are compositionally identical but sequentially distinct have been designed to study the impact of morphology and hydrophobicity on heme coordination and function.},
doi = {10.1039/c7ob01081h},
journal = {Organic and Biomolecular Chemistry},
number = 32,
volume = 15,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2017},
month = {Sun Jan 01 00:00:00 EST 2017}
}
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