| Original Articles |
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Scaling Behaviour of Conserved Sites in Protein Families |
| LI Jie;WANG Jun;WANG Wei |
| National Laboratory of Solid State Microstructure, Institute of Biophysics, and Department of Physics, Nanjing University, Nanjing 210093 |
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| Cite this article: |
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LI Jie, WANG Jun, WANG Wei 2005 Chin. Phys. Lett. 22 1274-1277 |
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Abstract Base on the database of families of structurally similar proteins, a statistical study is made on the scaling behaviour of occupying probabilities of conserved sites (Pc) in various protein families. A power-law decrease of Pc with the increasing protein-chain length Lf is found. This is related to the power-law scaling behaviour of the occurring probabilities of local contact interactions (Plocal) between residues. In addition, applying residue grouping, we find the same scaling behaviour when the number of residue types is more than 12, indicating that 12 residue types are enough to present the complexity of proteins.
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| Keywords:
87.10.+e
87.15.Cc
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Published: 01 May 2005
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| PACS: |
87.10.+e
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87.15.Cc
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(Folding: thermodynamics, statistical mechanics, models, and pathways)
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