Thermal unfolding of ribonuclease T1 studied by multi-dimensional NMR spectroscopy
Gespeichert in:
Verfasser / Beitragende:
[Hisae Matsuura, Sakurako Shimotakahara, Chiseko Sakuma, Mitsuru Tashiro, Heisaburo Shindo, Kiwa Mochizuki, Akihiko Yamagishi, Masaki Kojima, Kenji Takahashi]
Ort, Verlag, Jahr:
2004
Enthalten in:
Biological Chemistry, 385/12(2004-12-01), 1157-1164
Format:
Artikel (online)
Online Zugang:
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| 024 | 7 | 0 | |a 10.1515/BC.2004.149 |2 doi |
| 035 | |a (NATIONALLICENCE)gruyter-10.1515/BC.2004.149 | ||
| 245 | 0 | 0 | |a Thermal unfolding of ribonuclease T1 studied by multi-dimensional NMR spectroscopy |h [Elektronische Daten] |c [Hisae Matsuura, Sakurako Shimotakahara, Chiseko Sakuma, Mitsuru Tashiro, Heisaburo Shindo, Kiwa Mochizuki, Akihiko Yamagishi, Masaki Kojima, Kenji Takahashi] |
| 520 | 3 | |a Thermal unfolding of ribonculease (RNase) T1 was studied by 1H nuclear Overhauser enhancement spectroscopy (NOESY) and 1H-15N heteronuclear single-quantum coherence (HSQC) NMR spectroscopy at various temperatures. Native RNase T1 is a single-chain molecule of 104 amino acid residues, and has a single α-helix and two β-sheets, A and B, which consist of two and five strands, respectively. Singular value decomposition analysis based on temperature-dependent HSQC spectra revealed that the thermal unfolding of RNase T1 can be described by a two-state transition model. The midpoint temperature and the change in enthalpy were determined as 54.0°C and 696kJ/mol, respectively, which are consistent with results obtained by other methods. To analyze the transition profile in more detail, we investigated local structural changes using temperature-dependent NOE intensities. The results indicate that the helical region starts to unfold at lower temperature than some β-strands (B3, B4, and B5 in β-sheet B). These β-strands correspond to the hydrophobic cluster region, which had been expected to be a folding core. This was confirmed by structure calculations using the residual NOEs observed at 56°C. Thus, the two-state transition of RNase T1 appears to involve locally different conformational changes. | |
| 540 | |a ©2004 by Walter de Gruyter Berlin New York | ||
| 690 | 7 | |a Biochemistry |2 nationallicence | |
| 690 | 7 | |a Molecular biology |2 nationallicence | |
| 690 | 7 | |a Cellular biology |2 nationallicence | |
| 690 | 7 | |a nuclear magnetic resonance |2 nationallicence | |
| 690 | 7 | |a residual structure |2 nationallicence | |
| 690 | 7 | |a ribonuclease T1 |2 nationallicence | |
| 690 | 7 | |a singular value decomposition |2 nationallicence | |
| 690 | 7 | |a thermal unfolding |2 nationallicence | |
| 700 | 1 | |a Matsuura |D Hisae |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | |
| 700 | 1 | |a Shimotakahara |D Sakurako |u School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | |
| 700 | 1 | |a Sakuma |D Chiseko |u School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | |
| 700 | 1 | |a Tashiro |D Mitsuru |u Department of Chemistry, Faculty of Science, Tokyo Metropolitan University, Minami-Osawa, Hachioji, Tokyo 192-0397, Japan |4 aut | |
| 700 | 1 | |a Shindo |D Heisaburo |u School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | |
| 700 | 1 | |a Mochizuki |D Kiwa |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | |
| 700 | 1 | |a Yamagishi |D Akihiko |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | |
| 700 | 1 | |a Kojima |D Masaki |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | |
| 700 | 1 | |a Takahashi |D Kenji |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | |
| 773 | 0 | |t Biological Chemistry |d Walter de Gruyter |g 385/12(2004-12-01), 1157-1164 |x 1431-6730 |q 385:12<1157 |1 2004 |2 385 |o bchm | |
| 856 | 4 | 0 | |u https://doi.org/10.1515/BC.2004.149 |q text/html |z Onlinezugriff via DOI |
| 908 | |D 1 |a research article |2 jats | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1515/BC.2004.149 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Matsuura |D Hisae |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Shimotakahara |D Sakurako |u School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Sakuma |D Chiseko |u School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tashiro |D Mitsuru |u Department of Chemistry, Faculty of Science, Tokyo Metropolitan University, Minami-Osawa, Hachioji, Tokyo 192-0397, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Shindo |D Heisaburo |u School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Mochizuki |D Kiwa |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Yamagishi |D Akihiko |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Kojima |D Masaki |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Takahashi |D Kenji |u School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Biological Chemistry |d Walter de Gruyter |g 385/12(2004-12-01), 1157-1164 |x 1431-6730 |q 385:12<1157 |1 2004 |2 385 |o bchm | ||
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