Relationship between local structural entropy and protein thermostability

Chen Hsiung Chan, Han Kuen Liang, Nai Wan Hsiao, Ming Tat Ko, Ping Chiang Lyu, Jenn Kang Hwang

Research output: Contribution to journalArticlepeer-review

57 Citations (Scopus)


We developed a technique to compute structural entropy directly front protein sequences. We explored the possibility of using structural entropy to identify residues involved in thermal stabilization of various protein families. Examples include methanococcal adenylate kinase, Ribonuclease HI and holocytochrome C551. Our results show that the positions of the largest structural entropy differences between wild type and mutant usually coincide with the residues relevant to thermostability. We also observed a good linear relationship between the average structural entropy and the melting temperatures for adenylate kinase and its chimeric constructs. To validate this linear relationship, we compiled a large dataset comprised of 1153 sequences and found that most protein families still display similar linear relationships. Our results suggest that the multitude of interactions involved in thermal stabilization may be generalized into the tendency of proteins to maintain local structural conservation. The linear relationship between structural entropy and protein thermostability should be useful in the study of protein thermal stabilization.

Original languageEnglish
Pages (from-to)684-691
Number of pages8
JournalProteins: Structure, Function and Genetics
Issue number4
Publication statusPublished - 2004 Dec 1

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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