Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins | Zendy

Łukasz Mioduszewski | Zendy; Bartosz Różycki | Zendy; Marek Cieplak | Zendy

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Pseudo-Improper-Dihedral Model for Intrinsically Disordered Proteins

Author(s) -

Łukasz Mioduszewski,

Bartosz Różycki,

Marek Cieplak

Publication year - 2020

Publication title -

journal of chemical theory and computation

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 2.001

H-Index - 185

eISSN - 1549-9626

pISSN - 1549-9618

DOI - 10.1021/acs.jctc.0c00338

Subject(s) - dihedral angle , parameterized complexity , molecular dynamics , millisecond , intrinsically disordered proteins , amino acid residue , computer science , biological system , simple (philosophy) , chemistry , biophysics , algorithm , computational chemistry , physics , peptide sequence , biology , biochemistry , hydrogen bond , philosophy , organic chemistry , epistemology , astronomy , molecule , gene

We present a new coarse-grained C α -based protein model with a nonradial multibody pseudo-improper-dihedral potential that is transferable, time-independent, and suitable for molecular dynamics. It captures the nature of backbone and side-chain interactions between amino acid residues by adapting a simple improper dihedral term for a one-bead-per-residue model. It is parameterized for intrinsically disordered proteins and applicable to simulations of such proteins and their assemblies on millisecond time scales.

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