Volume 43, Issue 42 pp. 5649-5651
Communication

Calibrated Calculation of Polyalanine Fractional Helicities from Circular Dichroism Ellipticities

Gabriel E. Job

Gabriel E. Job

Department of Chemistry, Room 18-296, Massachusetts Institute of Technology, Cambridge, MA 02139, USA, Fax: (+1) 617-258-7500

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Björn Heitmann Dr.

Björn Heitmann Dr.

Department of Chemistry, Room 18-296, Massachusetts Institute of Technology, Cambridge, MA 02139, USA, Fax: (+1) 617-258-7500

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Robert J. Kennedy Dr.

Robert J. Kennedy Dr.

Department of Chemistry, Room 18-296, Massachusetts Institute of Technology, Cambridge, MA 02139, USA, Fax: (+1) 617-258-7500

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Sharon M. Walker Dr.

Sharon M. Walker Dr.

Department of Chemistry, Room 18-296, Massachusetts Institute of Technology, Cambridge, MA 02139, USA, Fax: (+1) 617-258-7500

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Daniel S. Kemp Prof.

Daniel S. Kemp Prof.

Department of Chemistry, Room 18-296, Massachusetts Institute of Technology, Cambridge, MA 02139, USA, Fax: (+1) 617-258-7500

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First published: 20 October 2004
Citations: 15

This research was supported by the NSF CHE-0131250 and the NIH GM 13453 (S.M.W.).

Graphical Abstract

Maximally helical polyalanines, 9 to 24 residues in length, are used to calibrate the assignment of fractional helicity (FH) from circular dichroism ellipticities. Water-solubilizing, helix-stabilizing N- and C-caps induce FHs>0.9 in core polyalanine regions. Linear length regressions of peptide molar ellipticities (blue-green curves) yield slopes (red arrows) that define molar per-residue ellipticities of a fully helical alanine residue (red curve).

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