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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Autors principals:	Risako Kimura, Panyavut Aumpuchin, Shoya Hamaue, Takumi Shimomura, Takeshi Kikuchi
Format:	Artigo
Idioma:	Inglês
Publicat:	BMC 2020-04-01
Col·lecció:	BMC Molecular and Cell Biology
Matèries:	β-Trefoil fold Folding mechanism Inter-residue average distance statistics Conserved hydrophobic residues Gō-model simulation
Accés en línia:	http://link.springer.com/article/10.1186/s12860-020-00271-4
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