Secondary structure analyses performed using the DICHROWEB web server with the CONTINLL algorithm and reference data set 4.
figure
posted on 2012-10-04, 01:11 authored by Begoña O. Alén, Lidia Nieto, Uxía Gurriarán-Rodríguez, Carlos S. Mosteiro, Juan C. Álvarez-Pérez, María Otero-Alén, Jesús P. Camiña, Rosalía Gallego, Tomás García-Caballero, Manuel Martín-Pastor, Felipe F. Casanueva, Jesús Jiménez-Barbero, Yolanda PazosThe relative amounts of α-helix and β-sheet were determined by adding together the contributions from helix 1 plus helix 2 and strand 1 plus strand 2, respectively, whereas the amounts of β-turn and random structure were read directly from the output. The peptides clearly showed greater helicity in SDS than in PBS.
