The analysis of chemical shifts for Hα protons with respect to the random coil reference values showed a negative trend ( Figure 3 A), mainly, [ 75 , 76 ] that is characteristic of helical/turn conformations, more evident in the region between residues Y 7 and V 16 , including the cyclic arrangement of the stapled peptide.
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Structure-Activity Relationship Investigations of Novel Constrained Chimeric Peptidomimetics of SOCS3 Protein Targeting JAK2.
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