期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 105, 期 37, 页码 13865-13870出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0804512105
关键词
energy landscape theory; structure-based model; circular permutation
资金
- Ministry of Education, Culture, Sports, Science, and Technology, Japan
- 21st century Center of Excellence
- Grants-in-Aid for Scientific Research [20244068] Funding Source: KAKEN
Multidomain proteins are ubiquitous in both prokaryotic and eukaryotic proteomes. Study on protein folding, however, has concentrated more on the isolated single domains of proteins, and there have been relatively few systematic studies on the effects of domain-domain interactions on folding. We here discuss this issue by examining human gamma D-crystallin, spore coat protein S, and a tandem array of the R16 and R17 domains of spectrin as example proteins by using a structure-based model of folding. The calculated results consistently explain the experimental data on folding pathways and effects of mutational perturbations, supporting the view that the connectivity of two domains and the distribution of domain-domain interactions in the native conformation are factors to determine kinetic and equilibrium properties of cooperative folding.
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