Entropic Stabilization of Isolated β-Sheets.
Temperature-dependent electric deflection measurements have been performed for a series of unsolvated alanine-based peptides (Ac-WA-NH, where Ac = acetyl, W = tryptophan, A = alanine, and n = 3, 5, 10, 13, and 15). The measurements are interpreted using Monte Carlo simulations performed with a paral...
| Published in: | Journal of the American Chemical Society Vol. 127; no. 13; pp. 4675 - 4680 |
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| Main Authors: | , , , , |
| Format: | Article |
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American Chemical Society
4/6/2005
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| Online Access: | View this record in EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=16688497&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 16688497 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 4/6/2005 vid: 127 iid: 13 pid: 997 pub: American Chemical Society artinfo: ui: 16688497 10.1021/ja0437499 ppf: 4675 ppct: 5 formats: tig: atl: Entropic Stabilization of Isolated β-Sheets. aug: au: Dugourd, Philippe Antoine, Rodolphe Breaux, Gary Broyer, Michel Jarrold, Martin F. affil: Laboratoire de Spectrométrie Ionique et Moléculaire, UMR No. 5579, CNRS et Université Lyon 1, 43 bd du 11 novembre 1918, 69622 Villeurbanne Cedex, France. Chemistry Department, Indiana University, 800 East Kirkwood Avenue, Bloomington, Indiana 47405-7102. su: Alanine Peptides Tryptophan Temperature Proteins Amino acids sug: subj: Alanine Peptides Tryptophan Temperature Proteins Amino acids ab: Temperature-dependent electric deflection measurements have been performed for a series of unsolvated alanine-based peptides (Ac-WA-NH, where Ac = acetyl, W = tryptophan, A = alanine, and n = 3, 5, 10, 13, and 15). The measurements are interpreted using Monte Carlo simulations performed with a parallel tempering algorithm. Despite alanine's high helix propensity in solution, the results suggest that unsolvated Ac-WA-NH peptides with n>10 adopt β-sheet conformations at room temperature. Previous studies have shown that protonated alanine-based peptides adopt helical or globular conformations in the gas phase, depending on the location of the charge. Thus, the charge more than anything else controls the structure. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2005 holdings: @attributes: islocal: N |
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