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Unifying features in protein-folding mechanisms.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America . 11/11/2003, Vol. 100 Issue 23, p13286-13291. 6p. - Publication Year :
- 2003
-
Abstract
- We compare the folding of representative members of a protein superfamily by experiment and simulation to investigate common features in folding mechanisms. The homeodomain superfamily of three-helical, single-domain proteins exhibits a spectrum of folding processes that spans the complete transition from concurrent secondary and tertiary structure formation (nucleation-condensation mechanism) to sequential secondary and tertiary formation (framework mechanism). The unifying factor in their mechanisms is that the transition state for (un)folding is expanded and very native-like, with the proportion and degree of formation of secondary and tertiary interactions varying. There is a transition, or slide, from the framework to nucleation-condensation mechanism with decreasing stability of the secondary structure. Thus, framework and nucleation-condensation are different manifestations of an underlying common mechanism. [ABSTRACT FROM AUTHOR]
- Subjects :
- *PROTEIN folding
*NUCLEATION
*CONDENSATION
*PROTEINS
Subjects
Details
- Language :
- English
- ISSN :
- 00278424
- Volume :
- 100
- Issue :
- 23
- Database :
- Academic Search Index
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 11681938
- Full Text :
- https://doi.org/10.1073/pnas.1835776100