Analyses of the folding sites of irregular β-trefoil fold proteins through sequence-based techniques and Gō-model simulations

Analyses of the folding sites of irregular β-trefoil fold proteins through sequence-based techniques and Gō-model simulations

Abstract Background The details of the folding mechanisms have not yet been fully understood for many proteins, and it is believed that the information on the folding mechanism of a protein is encoded in its amino acid sequence. β-trefoil proteins are known to have the same 3D scaffold, namely, a th...

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Bibliographic Details
Main Authors: Risako Kimura, Panyavut Aumpuchin, Shoya Hamaue, Takumi Shimomura, Takeshi Kikuchi
Format: Article
Language:English
Published: BMC 2020-04-01
Series:BMC Molecular and Cell Biology
Subjects:
β-Trefoil fold
Folding mechanism
Inter-residue average distance statistics
Conserved hydrophobic residues
Gō-model simulation
Online Access:http://link.springer.com/article/10.1186/s12860-020-00271-4

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http://link.springer.com/article/10.1186/s12860-020-00271-4

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