Deconvoluting Protein (Un)folding Structural Ensembles Using X-Ray Scattering, Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulation
Fig 3
Agreement of HN-N RDCs to EnHD crystal structure at increasing temperatures.
The Cornilescu Q factors were calculated using a sliding window from ‘Window start’ to ‘Window end’ to estimate the agreement of the given residue range. Q = 0.25 was used as the cut-off for the agreement [24]. At 20°C (a) and 30°C (b) EnHD is fully folded, and any chosen residue window displays perfect agreement with the crystal structure. At 40°C (c) the agreement for the 10–55 fragment is not present, but the HTH motif remains structured. This indicates that H1 must be undocked from H2/H3. C. At 55°C (d) around the thermal midpoint of denaturation, some HN-N RDCs for H2/H3 remain in agreement with the crystal structure.