A multicanonical molecular dynamics study on a simple bead-spring model for protein folding

Journal of the Physical Society of Japan

Volumn 70, Issue 5, 2001, Pages 1233-1236

  Isobe, Masaharu ^a,b   Shimizu, Hisashi ^a   Hiwatari, Yasuaki ^b  

^a SHINSHU UNIVERSITY   (Japan)

^b KANAZAWA UNIVERSITY   (Japan)

Author keywords

Bead spring model; Continuum model; Coulomb interaction; Hydrophobic interaction; Multicanonical molecular dynamics simulation; Protein folding; Solvent effect

Indexed keywords

EID: 0035626416     PISSN: 00319015     EISSN: None     Source Type: Journal    
DOI: 10.1143/JPSJ.70.1233     Document Type: Article

References (17)

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13. In Fig. 3, it turns out that this model protein has a minimum free energy in the region of the localized high probability. When the hydrophobic interaction becomes weaker, the region of the high probability extends over in RG-DME plane. This indicates that the conformation of minimum free energy is substantially degenerated.
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17. To our knowledge, experiments on protein folding in various solvents (such as ethanol) have not been studied yet. Our simulation must be useful in understanding the role of long-range interactions in an early stage of protein folding in different solutions.