Effects of pressure on the structure of metmyoglobin: Molecular dynamics predictions for pressure unfolding through a molten globule intermediate

• Published in: Protein science Vol. 7; no. 11; pp. 2301 - 2313
• Main Authors: Floriano, Wely B., Nascimento, Marco A. C., Domont, Gilberto B., Goddard, William A.
• Format: Journal Article
• Language: English
• Published: Bristol Cold Spring Harbor Laboratory Press 01.11.1998
• Subjects: Amino Acid Sequence; Computer Simulation; Hydrogen Bonding; Metmyoglobin - chemistry; Models, Molecular; molecular dynamics; Molecular Sequence Data; molten globule; myoglobin; Pressure; Protein Conformation; Protein Folding; Protein Structure, Secondary; Sequence Alignment; Solvents; Temperature; Tryptophan - chemistry; unfolding

We investigated the pathway for pressure unfolding of metmyoglobin using molecular dynamics (MD) for a range of pressures (0. 1 MPa to 1. 2 GPa) and a temperature of 300 K. We find that the unfolding of metmyoglobin proceeds via a two‐step mechanism native → molten globule intermediate → unfolded, w...