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Quantitative Biology > Biomolecules

arXiv:q-bio/0512020 (q-bio)
[Submitted on 9 Dec 2005 (v1), last revised 28 Dec 2005 (this version, v2)]

Title:Diversity in Free Energy Landscape of Proteins with the Same Native Topology

Authors:Hiroo Kenzaki, Macoto Kikuchi
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Abstract: In order to elucidate the role of the native state topology and the stability of subdomains in protein folding, we investigate free energy landscape of human lysozyme, which is composed of two subdomains, by Monte Carlo simulations. A realistic lattice model with Go-like interaction is used. We take the relative interaction strength (stability, in other word) of two subdomains as a variable parameter and study the folding process. A variety of folding process is observed and we obtained a phase diagram of folding in terms of temperature and the relative stability. Experimentally-observed diversity in folding process of c-type lysozimes is thus understood as a consequence of the difference in the relative stability of subdomains.
Comments: 4 pages, 3 figures
Subjects: Biomolecules (q-bio.BM); Soft Condensed Matter (cond-mat.soft); Biological Physics (physics.bio-ph)
Cite as: arXiv:q-bio/0512020 [q-bio.BM]
  (or arXiv:q-bio/0512020v2 [q-bio.BM] for this version)
  https://doi.org/10.48550/arXiv.q-bio/0512020
Journal reference: Chem. Phys. Lett. 427 (2006) 414-417
Related DOI: https://doi.org/10.1016/j.cplett.2006.05.112

Submission history

From: Hiroo Kenzaki [view email]
[v1] Fri, 9 Dec 2005 12:51:51 UTC (176 KB)
[v2] Wed, 28 Dec 2005 09:10:10 UTC (177 KB)
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