A model peptide with enhanced helicity
Biochemistry1991Vol. 30(17), pp. 4245–4248
Citations Over TimeTop 10% of 1991 papers
Abstract
The sequence of a model monomeric peptide, acetylA(EAAAK)3Aamide was altered to expedite measurement of peptide concentration and to enhance its fractional helical content. Replacement of the N-terminal alanine residue with a tryptophan residue provides a convenient chromophore for measurement of peptide concentration without diminishing the helical content. Replacement of the three lysine residues with arginine residues enhances the helical content without loss of their electrostatic contributions. Increasing the number of EAAAR sequence units in the peptide acetylW(EAAAR)nAamide from three to five indicates that the spectral features anticipated for a completely helical peptide are closely approached.
Related Papers
- → Synthesis of Chromophores with Extremely High Electro-optic Activity. 1. Thiophene-Bridge-Based Chromophores(2002)116 cited
- → Using phenoxazine and phenothiazine as electron donors for second-order nonlinear optical chromophore: Enhanced electro-optic activity(2014)55 cited
- → The design of nonlinear optical chromophores exhibiting large electro-optic activity and high thermal stability: The role of donor groups(2016)33 cited
- → Single Oligomer Spectra Probe Chromophore Nanoenvironments of Tetrameric Fluorescent Proteins(2006)20 cited
- → Factors affecting the estimation of the relative amount of chromophore and chromophore area by the two-wavelength method of patau and ornstein(1976)7 cited