Abstract
Proteins of both hyperthermophilic and mesophilic microorganisms generally constitute from the same 20 amino acids; however, the extent of thermal tolerance of any given protein is an inherent property of its amino acid sequence. The present study is the first to report a rapid method for predicting Tm (melting temperature), the temperature at which 50% of the protein is unfolded, directly from protein sequences (the Tm Index program is available at http://tm.life.nthu.edu.tw/). We examined 75 complete microbial genomes using the Tm Index, and the analysis clearly differentiated hyperthermophilic from mesophilic microorganisms on this global genomic basis. These results are consistent with the previous hypothesis that hyperthermophiles express a greater number of high Tm proteins compared with mesophiles. The Tm Index will be valuable for modifying existing proteins (enzymes, protein drugs and vaccines) or designing novel proteins having a desired melting temperature.
| Original language | English |
|---|---|
| Pages (from-to) | 445-450 |
| Number of pages | 6 |
| Journal | Computational Biology and Chemistry |
| Volume | 33 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2009 Dec 1 |
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All Science Journal Classification (ASJC) codes
- Structural Biology
- Biochemistry
- Organic Chemistry
- Computational Mathematics
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Predicting melting temperature directly from protein sequences. / Ku, Tienhsiung; Lu, Peiyu; Chan, Chenhsiung; Wang, Tsusheng; Lai, Szuming; Lyu, Pingchiang; Hsiao, Nai-Wan.
In: Computational Biology and Chemistry, Vol. 33, No. 6, 01.12.2009, p. 445-450.Research output: Contribution to journal › Article
TY - JOUR
T1 - Predicting melting temperature directly from protein sequences
AU - Ku, Tienhsiung
AU - Lu, Peiyu
AU - Chan, Chenhsiung
AU - Wang, Tsusheng
AU - Lai, Szuming
AU - Lyu, Pingchiang
AU - Hsiao, Nai-Wan
PY - 2009/12/1
Y1 - 2009/12/1
N2 - Proteins of both hyperthermophilic and mesophilic microorganisms generally constitute from the same 20 amino acids; however, the extent of thermal tolerance of any given protein is an inherent property of its amino acid sequence. The present study is the first to report a rapid method for predicting Tm (melting temperature), the temperature at which 50% of the protein is unfolded, directly from protein sequences (the Tm Index program is available at http://tm.life.nthu.edu.tw/). We examined 75 complete microbial genomes using the Tm Index, and the analysis clearly differentiated hyperthermophilic from mesophilic microorganisms on this global genomic basis. These results are consistent with the previous hypothesis that hyperthermophiles express a greater number of high Tm proteins compared with mesophiles. The Tm Index will be valuable for modifying existing proteins (enzymes, protein drugs and vaccines) or designing novel proteins having a desired melting temperature.
AB - Proteins of both hyperthermophilic and mesophilic microorganisms generally constitute from the same 20 amino acids; however, the extent of thermal tolerance of any given protein is an inherent property of its amino acid sequence. The present study is the first to report a rapid method for predicting Tm (melting temperature), the temperature at which 50% of the protein is unfolded, directly from protein sequences (the Tm Index program is available at http://tm.life.nthu.edu.tw/). We examined 75 complete microbial genomes using the Tm Index, and the analysis clearly differentiated hyperthermophilic from mesophilic microorganisms on this global genomic basis. These results are consistent with the previous hypothesis that hyperthermophiles express a greater number of high Tm proteins compared with mesophiles. The Tm Index will be valuable for modifying existing proteins (enzymes, protein drugs and vaccines) or designing novel proteins having a desired melting temperature.
UR - http://www.scopus.com/inward/record.url?scp=70449708890&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=70449708890&partnerID=8YFLogxK
U2 - 10.1016/j.compbiolchem.2009.10.002
DO - 10.1016/j.compbiolchem.2009.10.002
M3 - Article
C2 - 19896904
AN - SCOPUS:70449708890
VL - 33
SP - 445
EP - 450
JO - Computational Biology and Chemistry
JF - Computational Biology and Chemistry
SN - 1476-9271
IS - 6
ER -