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| Type |
Poster Presentation |
| Area |
생명화학 |
| Room No. |
포스터발표장 |
| Time |
4월 21일 (금요일) 13:00~14:30 |
| Code |
BIO.P-315 |
| Subject |
Structural and Dynamic Features of Cold Shock Protein from Colwellia psychrerythraea, studied by NMR spectroscopy |
| Authors |
이영준, 김양미*
건국대학교 생명공학과, Korea
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| Abstract |
When temperature drops below the growth temperature, cold-shock proteins (Csps) are expressed. Cold-shock proteins can bind to single-stranded nucleic acids, and this ability allows them to act as RNA chaperones. Colwellia psychrerythraea is a Gram-negative psychrophile. The bacteria can survive even in freezing temperature of polar regions. Although cold-shock proteins from various organisms have dramatic differences in their meting temperatures, their amino acid sequences and three-dimensional structures share high similarity. Here, we investigated the structure and dynamics of C. psychrerythraea Csp (Cp-Csp). Cp-Csp contains five β-strands forming barrel structure with hydrophobic core. Psychrophilic Cp-Csp defolds at lower temperature(37℃) than its mesophilic and thermophilic homologues do. By analysing 3D structure and the backbone dynamics results, it revealed that Cp-Csp has higher structural flexibility and less hydrophobic packing compared to psychrotrophic L. monocytogenes Csp and thermophilic T. aquaticus Csp. These features, as well as the number of salt bridges, are seems to be key reasons of low thermostability of Cp-Csp. This implies that the large conformational flexibility makes the protein to accommodate nucleic acids more easily at extremely low temperature, which is important factor for RNA chaperone function and the cold adaptation of C. psychrerythraea. |
| E-mail |
lyj7956@konkuk.ac.kr |
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119th General Meeting of the KCS