Influence of substrate pattern on the adsorption of HP lattice proteins
- Univ. of Georgia, Athens, GA (United States)
- Eidgenoessische Technische Hochschule (ETH), Zurich (Switzerland)
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
With the highly simplified hydrophobic-polar model representation of a protein, we can study essential qualitative physics without an unnecessarily large computational overhead. Using Wang-Landau sampling in conjunction with a set of efficient Monte Carlo trial moves, we studied the adsorption of short HP lattice proteins on various simple patterned substrates and in particular for checkered patterned surfaces. In this work, a set of single-site mutated HP proteins is used to investigate the role of hydrophobicity of a protein chain and surface pattern for substrates with various pattern cell sizes relative to the protein’s native configuration. For most cases, we found that the adsorption transition occurs at a lower temperature, while the hydrophobic core formation is less affected. Additionally, the flattening procedure after the HP protein is adsorbed is more sensitive to the change in surface patterns and single-site mutations. These observations stay valid for both strongly and weakly attractive surfaces.
- Research Organization:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Oak Ridge Leadership Computing Facility (OLCF)
- Sponsoring Organization:
- USDOE Office of Science (SC); National Science Foundation (NSF)
- Grant/Contract Number:
- AC05-00OR22725; PHY130014; OCI-0904685
- OSTI ID:
- 1649666
- Journal Information:
- Molecular Simulation, Vol. 44, Issue 12; ISSN 0892-7022
- Publisher:
- Taylor & FrancisCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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