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Topological determinants of protein unfolding rates
Author(s) -
Jung Jaewoon,
Lee Jooyoung,
Moon HieTae
Publication year - 2004
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20324
Subject(s) - protein folding , contact order , native state , topology (electrical circuits) , folding (dsp implementation) , protein structure , enhanced data rates for gsm evolution , chemistry , physics , chemical physics , crystallography , biophysics , mathematics , computer science , combinatorics , biology , biochemistry , artificial intelligence , electrical engineering , engineering
For proteins that fold by two‐state kinetics, the folding and unfolding processes are believed to be closely related to their native structures. In particular, folding and unfolding rates are influenced by the native structures of proteins. Thus, we focus on finding important topological quantities from a protein structure that determine its unfolding rate. After constructing graphs from protein native structures, we investigate the relationships between unfolding rates and various topological quantities of the graphs. First, we find that the correlation between the unfolding rate and the contact order is not as prominent as in the case of the folding rate and the contact order. Next, we investigate the correlation between the unfolding rate and the clustering coefficient of the graph of a protein native structure, and observe no correlation between them. Finally, we find that a newly introduced quantity, the impact of edge removal per residue , has a good overall correlation with protein unfolding rates. The impact of edge removal is defined as the ratio of the change of the average path length to the edge removal probability. From these facts, we conclude that the protein unfolding process is closely related to the protein native structure. Proteins 2005. © 2004 Wiley‐Liss, Inc.