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

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...

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Bibliographic Details
Published inProtein 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
LanguageEnglish
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
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Summary: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, where the molten globule forms at 700 MPa. The simulation describes qualitatively the experimental behavior of metmyoglobin under pressure. We find that unfolding of the alpha‐helices follows the sequence of migrating hydrogen bonds (i, i + 4) → (i, i + 2).
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ISSN:0961-8368
1469-896X
DOI:10.1002/pro.5560071107