Length-dependent stability and strand length limits in antiparallel beta -sheet secondary structure.
SEQUENCE RESIDUE 12 IN THE PEPTIDE IS ORNITHINE. FOR MODELLING, LYSINE WAS USED IN PLACE OF ORNITHINE FOR EASE OF CALCULATION.
The peptide was synthesized by solid phase peptide synthesis.
NOE intensities were qualitatively assigned to be strong, medium, weak or very weak, and assigned constraints of 3, 4, 5, and 6 respectively; a total of 32 restraints were used for DP-TT2. Restraints were checked using "distance check" function within DYANA which showed there were no "lonely" or possibly misassigned NOEs which could unduly influence the final conformation. DYANA was used to generate 500 random structures, which were subsequently annealed. The best 10 structures (fewest restraint violations) were selected. This entry contains the minimized average structure.