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. Author manuscript; available in PMC: 2019 Apr 15.
Published in final edited form as: J Phys Chem B. 2018 Aug 8;122(49):11137–11146. doi: 10.1021/acs.jpcb.8b05982

Figure 3.

Figure 3.

CaM-binding motifs in nSH2 and cSH2 domains. (A) One CaM-binding motif in the cSH2 domain at residues 664–679 exhibits a 100% β-sheet structure, and (B) another at residues 684–699 adopts a dominant α-helix conformation. (C) The single CaM-binding motif in the nSH2 domain at residues 389–404 has mixed α-helix, random coil, and β-sheet structures.