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. Author manuscript; available in PMC: 2018 Dec 5.
Published in final edited form as: Biochemistry. 2017 Nov 21;56(48):6343–6354. doi: 10.1021/acs.biochem.7b00970

Figure 4:

Figure 4:

Proton line broadening spectra for PAR3 and PAR3G peptides in the presence of prothrombin and PPACK-thrombin. All NMR samples were in 25mM H3PO4, 150 mM NaCl, 0.2 mM EDTA and 10 % D2O (pH 6.5). (A) 1D 1H-NMR spectrum for 1 mM PAR3 (44– 56) peptide in solution (B) 1D 1H-NMR spectrum for 1mM PAR3 (44–56) peptide in the presence of 74 μM ProT (C) 1D 1H-NMR spectrum for 1 mM PAR3 (44–56) peptide in the presence of 77 μM PPACK-IIa (D) 1D NMR spectmm for 1 mM PAR3G (44– 56) peptide in solution (E) 1D NMR spectrum for 960 μM PAR3G (44–56) peptide in the presence of 76 μM ProT. (F) 1D NMR spectrum for 1000 mM PAR3G (44–56) peptide in the presence of 76 μM PPACK-IIa. Line broadening was observed for residues of PAR3 (44–56) and PAR3G (44–56) when either peptide was bound to prothrombin and PPACK-Ha. The amide protons that were later selected for HSQC titrations are labeled.