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Figure 3 | BMC Biochemistry

Figure 3

From: NMR characterisation of the minimal interacting regions of centrosomal proteins 4.1R and NuMA1: effect of phosphorylation

Figure 3

Tendency of 4.1R-CTD64 to adopt an α-helix conformation. A: Conformational Δδ13Cα (Δδ13Cα = δ13Cα, experimental- δ13Cα, random coil, ppm) chemical shifts as a function of sequence. Positive values indicate α-helix structure. B: Conformational Δδ13Cβ (Δδ13Cβ = δ13Cβ, experimental- δ13Cβ, random coil, ppm) chemical shifts as a function of sequence. Negative values indicate α-helix structure. C: Theoretical prediction of helical percentage at 5°C and pH 5.0 by AGADIR [23] as a function of residue number.

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