random conformation
1.The random conformation of PMALM blocks was verified by CD spectra and the linear relationship between the specific rotation and the polarity of CH_3OH/CCl_4 mixed solvent.
2.When voltage was 12kv, at different C-SD, The content of random /α-helical conformation in ERS improved with the C-SD increasing, but the crystallinity increased only slightly then decreased sharply.
3.Improvement in thermostability of enzymes by protein engineering may introduce Pro at suitable β|turns and random coils. The rigid pyrrolidine ring can make the conformation of surroundings to be more reasonable by reducing the backbone unfolding entropy of proteins.
5.1. Influences of low pH and NBS modification of Trp241 upon conformational changes in 33 kDa proteinThe studies of both circular dichroism (CD) and fluorescence spectra showed that upon decreasing pH from 6.2 to 2.5, the conformation of soluble 33 kDa protein changed significantly, with an increase of random coil.
