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|
| Type |
Poster Presentation |
| Area |
Physical Chemistry |
| Room No. |
Event Hall |
| Time |
4월 20일 (금요일) 11:00~12:30 |
| Code |
PHYS.P-123 |
| Subject |
Cold Denaturation of Ubiquitin Associated Domain Peptide |
| Authors |
CheongHa Lim, Manho Lim*
Department of Chemistry, Pusan National University, Korea
|
| Abstract |
FT-IR spectroscopy was used to investigate cold denaturation of ubiquitin associated domain peptide (UBA(2)) composed of 3 α-helix by observing amide Ⅰ band at 1600~1700 cm-1, known to be sensitive to the secondary structure of peptide, in temperature range from 323K to 263 K. The solution consisted of 1.7 mM protein with 0.1 M Tri(2-carboxyethyl)phosphine (TCEP)-HCl, 2 M denaturant, and 0.4 M phosphate buffer in D2O (pD=6.4). TCEP was added to prevent the peptide from making dimer by breaking disulfide bond. As temperature decreases from 293 K to 263 K, the band near 1650 cm-1 decreases and that near 1620 cm-1 increases, indicating that α-helix of the peptide is getting loose and the content of the β sheet increases. Evidently, as UBA(2) cold denatures, α-helix unfolds and β sheet forms, suggesting that cold denaturation is not a simple randomization of the secondary structure but a systematic variation of the structure. Cold denaturation will be compared with thermal denaturation and the detailed variation in the structure will be accessed by molecular dynamics simulation. |
| E-mail |
ch.femto@gmail.com |
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121st General Meeting of the KCS