Please use this identifier to cite or link to this item:
|Title:||Thermodynamic analysis of protein sequence-structure relationships in monomer and dimer forms|
|Authors:||Li, Z.R. |
|Citation:||Li, Z.R., Liu, G.R., Cheng, Y. (2005-08-15). Thermodynamic analysis of protein sequence-structure relationships in monomer and dimer forms. Physica A: Statistical Mechanics and its Applications 354 (1-4) : 381-392. ScholarBank@NUS Repository. https://doi.org/10.1016/j.physa.2005.03.006|
|Abstract:||Two-dimensional lattice model is employed to analyze the sequence-structure relationships between HP and YhHX protein sequences and compact structures in monomer and homodimer forms. Our results show that most structures are encoded by normal and prion protein sequences, and about one-third of the protein sequences are potentially able to refold from its native monomer conformation to alternative ones upon dimerization thermodynamically. Such findings partially reflect the existences of the dimer and oligomer protein structures in living organism and the occurrence of pathologic dimerization or aggregation of monomer proteins. It is observed that protein sequences differ drastically in the number of strains. Statistically, the number of protein sequences decreases exponentially with the number of strains. Calculations using various energy parameters show that the expected value of maximum number of strains for a 16-residue sequence is about its length. © 2005 Elsevier B.V. All rights reserved.|
|Source Title:||Physica A: Statistical Mechanics and its Applications|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on May 18, 2018
WEB OF SCIENCETM
checked on Mar 27, 2018
checked on May 12, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.