Ontology type: schema:ScholarlyArticle
1987-04
AUTHORSKevin R. Shoemaker, Peter S. Kim, Eunice J. York, John M. Stewart, Robert L. Baldwin
ABSTRACTCharged groups play a critical role in the stability of the helix formed by the isolated C-peptide (residues 1–13 of ribonuclease A) in aqueous solution. One charged-group effect may arise from interactions between charged residues at either end of the helix and the helix dipole. We report here that studies of C-peptide analogues support the helix dipole model, and provide further evidence for the importance of electrostatic interactions not included in the Zimm–Bragg model for α-helix formation. More... »
PAGES563-567
http://scigraph.springernature.com/pub.10.1038/326563a0
DOIhttp://dx.doi.org/10.1038/326563a0
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/3561498
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