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Accurate protein-peptide titration experiments by nuclear magnetic resonance using low-volume samples

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Academic year: 2021

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Fig. 1 The titration protocol presented here is illustrated with data originating from an interaction study between a model peptide from the proline-rich region of the RAR γ NTD and the third SH3 domain of the human Vinexin β [8]
Fig. 2 1D proton spectrum of a mixture between a model peptide (sequence P 5 VP 5 RVYK) corresponding to the proline-rich region of the RAR γ NTD and the tryptophan solution of known concentration
Fig. 3 Preparation of capillary tubes (left) for 1 H– 15 N HSQC measurements (right). The insert shows a close-up on the effect of increasing amounts of peptide on the cross peak corresponding to the backbone amide proton of Tryptophan 42, which is located
Fig. 4 Least-square fit of the chemical shifts perturbation data measured for the interaction between the P 5 VP 5 RVYK model peptide and the Vinexin β SH3.3 domain

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