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Folding of Small Helical Proteins Assisted by Small-Angle X-Ray Scattering Profiles
- Source :
-
Structure . Nov2005, Vol. 13 Issue 11, p1587-1597. 11p. - Publication Year :
- 2005
-
Abstract
- Summary: This paper reports a computational method for folding small helical proteins. The goal was to determine the overall topology of proteins given secondary structure assignment on sequence. In doing so, a Monte Carlo protocol, which combines coarse-grained normal modes and a Hamiltonian at a different scale, was developed to enhance sampling. In addition to the knowledge-based potential functions, a small-angle X-ray scattering (SAXS) profile was also used as a weak constraint for guiding the folding. The algorithm can deliver structural models with overall correct topology, which makes them similar to those of 5∼6 Å cryo-EM density maps. The success could contribute to make the SAXS technique a fast and inexpensive solution-phase experimental method for determining the overall topology of small, soluble, but noncrystallizable, helical proteins. [Copyright &y& Elsevier]
- Subjects :
- *X-ray scattering
*BIOMOLECULES
*TOPOLOGY
*PARTIAL differential equations
Subjects
Details
- Language :
- English
- ISSN :
- 09692126
- Volume :
- 13
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- Structure
- Publication Type :
- Academic Journal
- Accession number :
- 19010634
- Full Text :
- https://doi.org/10.1016/j.str.2005.07.023