Packing helices in proteins by global optimization of a potential energy function
2003
An efficient method has been developed for packing α-helices in proteins. It treats α-helices as rigid bodies and uses a simplified Lennard–Jones potential with Miyazawa–Jernigan contact-energy parameters to describe the interactions between the α-helical elements in this coarse-grained system. Global conformational searches to generate packing arrangements rapidly are carried out with a Monte Carlo-with-minimization type of approach. The results for 42 proteins show that the approach reproduces native-like folds of α-helical proteins as low-energy local minima of this highly simplified potential function.
Keywords:
- Correction
- Source
- Cite
- Save
- Machine Reading By IdeaReader
19
References
39
Citations
NaN
KQI