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In the former solvent, all peptides investigated were shown to populate the 3<jats:sub>10<\/jats:sub>\u2010helix conformation, whereas in chloroform the two shortest members of the series (n = 1 and n = 2) adopt predominantly the 2.0<jats:sub>5<\/jats:sub>\u2010helix. Interestingly, for the longest components (n = 3 to n = 5) in this latter solvent, an equilibrium between the 2.0<jats:sub>5<\/jats:sub>\u2010 and 3<jats:sub>10<\/jats:sub>\u2010helices takes place, the latter conformation becoming progressively more populated as the peptide main\u2010chain length increases. Time\u2010resolved fluorescence (TRF) experiments and molecular mechanics (MM) calculations were used in a combined approach to analyze the ET efficiencies and to associate a specific conformer (from MM) to an experimentally determined ET rate constant (from TRF). Therefore, because of the high sensitivity of the ET process to the D\u00b7\u00b7\u00b7A distance, ET can be used as a kinetic spectroscopic ruler, allowing for the characterization of the transition from a pure 3<jats:sub>10<\/jats:sub>\u2010helix conformation to a 2.0<jats:sub>5<\/jats:sub>\u2010\/3<jats:sub>10<\/jats:sub>\u2010helix equilibrium for the longest Deg homo\u2010peptides of this series upon changing the solvent from acetonitrile to chloroform. To our knowledge, this is the first time that the electronic coupling factor \u03b2 for ET across a peptide chain in the 2.0<jats:sub>5<\/jats:sub>\u2010helix conformation is provided. \u00a9 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 100: 51\u201363, 2013.<\/jats:p>","DOI":"10.1002\/bip.22190","type":"journal-article","created":{"date-parts":[[2012,11,26]],"date-time":"2012-11-26T12:13:59Z","timestamp":1353932039000},"page":"51-63","source":"Crossref","is-referenced-by-count":15,"title":["Looking for the peptide 2.0<sub>5<\/sub>\u2010helix: A solvent\u2010 and main\u2010chain length\u2010dependent conformational switch probed by electron transfer across c<sup>\u03b1,\u03b1<\/sup>\u2010diethylglycine 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