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CHAINS OF ALTERNATING SULFUR AND π‐BONDED ATOMS IN EIGHT SMALL PROTEINS

Morgan, Richard S., Tatsch, Clinton E., Gushard, Robert H., Mcadon, John M., Warme, Paul K.·1978·International Journal of Peptide and Protein Research

Abstract

This paper demonstrates the existence of regions in eight small globular proteins in which the side chains of sulfur‐containing amino acids (cysteine and methionine) alternate in space with side chains of aromatic amino acids (histidine, phenylalanine, tryptophan and tyrosine). The proteins are: rubredoxin, high potential iron protein, cytochrome c, flavodoxin, deoxyhemoglobin, trypsin inhibitor, ribonuclease‐S, and lysozyme. The sulfur‐φ‐bonded ‘chains’ involve a minimum of five and a maximum of 10 amino acids, and contain the most polarizable atoms within proteins. S‐φ‐chains give extra stability to the folding of proteins; they may also afford paths for the step‐wise movement of electrons.

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Metadata

Authors
Morgan, R. S., Tatsch, C. E., Gushard, R. H., Mcadon, J. M., & Warme, P. K.
Venue
International Journal of Peptide and Protein Research
Publisher
Wiley
Published
1978-03
Volume
11
Issue
3
Pages
209-217
ISSN
0367-8377 (ISSN-L)
OpenAlex
W2043885312
Cited by
174
References
0
FWCI
1.61
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: CHAINS OF ALTERNATING SULFUR AND π‐BONDED ATOMS IN EIGHT SMALL PROTEINS. https://app.cochat.ai/papers/10.1111/j.1399-3011.1978.tb02841.x
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Morgan, R. S., Tatsch, C. E., Gushard, R. H., Mcadon, J. M., & Warme, P. K. (1978). CHAINS OF ALTERNATING SULFUR AND π‐BONDED ATOMS IN EIGHT SMALL PROTEINS. International Journal of Peptide and Protein Research. https://doi.org/10.1111/j.1399-3011.1978.tb02841.x

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.