期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 15, 页码 5933-5938出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1216589110
关键词
denaturing mechanism; protein unfolding; random coil; ensemble simulation
资金
- Ministerio de Economia y Competitividad-Spain [CTQ2009-08850, BIO2012-32868]
- Marato de TV3 [102030]
- European Research Council-Advanced grant
- Institut Nacional de Bioinformatica
- Consolider E-Science Project
- Framework VII Scalalife Project
- Fundacion Marcelino Botin
- ICREA Funding Source: Custom
We present here the characterization of the structural, dynamics, and energetics of properties of the urea-denatured state of ubiquitin, a small prototypical soluble protein. By combining state-of-the-art molecular dynamics simulations with NMR and small-angle X-ray scattering data, we were able to: (i) define the unfolded state ensemble, (ii) understand the energetics stabilizing unfolded structures in urea, (iii) describe the dedifferential nature of the interactions of the fully unfolded proteins with urea and water;and (iv) characterize the early stages of protein refolding when chemically denatured proteins are transferred to native conditions. The results presented herein are unique in providing a complete picture of the chemically unfolded state of proteins and contribute to deciphering the mechanisms that stabilize the native state of proteins, as well as those that maintain them unfolded in the presence of urea.
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