The use of pressure-jump relaxation kinetics to study protein folding landscapes
文献类型：期刊论文
| 作者 | Torrent, J; Font, J; Herberhold, H; Marchal, S; Ribo, M; Ruan, KC; Winter, R; Vilanova, M; Lange, R |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| 出版日期 | 2006 |
| 卷号 | 1764期号:3页码:489-496 |
| 关键词 | high pressure pressure jump protein folding relaxation kinetics |
| 通讯作者 | Lange, R (reprint author), Univ Montpellier 2, INSERM, U710, CC105,Pl Eugene Bataillon, F-34095 Montpellier 5, France.,lange@montp.inserm.fr |
| 英文摘要 | Pressure-jump induced relaxation kinetics can be used to study both protein unfolding and refolding. These processes can be initiated by upward and downward pressure-jumps of amplitudes of a few 10 to 100 MPa, with a dead-time on the order of milliseconds. In many cases, the relaxation times can be easily determined when the pressure cell is connected to a spectroscopic detection device, Such as a spectrofluorimeter. Adiabatic heating or cooling can be limited by small pressure-jump amplitudes and a special design of the sample cell. Here, we discuss the application of this method to four proteins: 33-kDa and 23-kDa proteins from photo-system 11, a variant of the green fluorescent protein, and a fluorescent variant of ribonuclease A. The thermodynamically predicted equivalency Of upward and downward pressure-jump induced protein relaxation kinetics for typical two-state folders was observed for the 33-kDa protein, only. In contrast, the three other proteins showed significantly different kinetics for pressure-jumps in opposite directions. These results cannot be explained by sequential reaction schemes. Instead, they are in line with a more complex free energy landscape involving multiple pathways. (c) 2006 Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | SPINACH PHOTOSYSTEM-II ; TRANSFORM INFRARED-SPECTROSCOPY ; RIBONUCLEASE-A ; STAPHYLOCOCCAL NUCLEASE ; PRION PROTEIN ; CONFORMATIONAL TRANSITIONS ; INITIATION SITE ; 33-KDA PROTEIN ; TEMPERATURE ; STATE |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000236839300019 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1689]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Torrent, J,Font, J,Herberhold, H,et al. The use of pressure-jump relaxation kinetics to study protein folding landscapes[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2006,1764(3):489-496. |
| APA | Torrent, J.,Font, J.,Herberhold, H.,Marchal, S.,Ribo, M.,...&Lange, R.(2006).The use of pressure-jump relaxation kinetics to study protein folding landscapes.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1764(3),489-496. |
| MLA | Torrent, J,et al."The use of pressure-jump relaxation kinetics to study protein folding landscapes".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1764.3(2006):489-496. |
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