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Protein folding: an antagonistic reaction of spontaneous folding and diffusion limited aggregation in nature
Author(s) -
Kan Lousing,
Chang ChiaChing
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a501-d
Subject(s) - folding (dsp implementation) , protein folding , downhill folding , chemistry , chemical physics , contact order , intermolecular force , phi value analysis , diffusion , process (computing) , path (computing) , biophysics , thermodynamics , physics , molecule , computer science , biology , biochemistry , organic chemistry , programming language , engineering , operating system , electrical engineering
Protein folding may follow a spontaneous process or a reaction‐path directed process. This difference may be caused by the variant folding transition boundaries due to intrinsic properties of proteins. A general first‐order‐like state‐transition model indicated that the protein might be trapped into an aggregated state when the folding path crosses the transition boundary. Both experimental study and molecular simulations indicated that protein within this transition region might contain intermolecular interactions. Therefore, a direct folding process may contain a combination of an antagonistic reaction of spontaneous folding and a diffusion limited aggregation. We would like to report in this paper a comparison between the conventional diffusion limited aggregation (DLA) process and folding time limited‐DLA process. Meanwhile the application of auto‐correlation function in time dependent biological studies will also be discussed. (Supported by National Science Council of The Executive Yuan and Academia Sinica)