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Engineering the Fullerene‐protein Interface by Computational Design: The Sum is More than its Parts
Author(s) -
Trozzi Francesco,
Marforio Tainah Dorina,
Bottoni Andrea,
Zerbetto Francesco,
Calvaresi Matteo
Publication year - 2017
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.201600127
Subject(s) - chemistry , fullerene , tryptophan , solvation , residue (chemistry) , van der waals force , tyrosine , histidine , polar , phenylalanine , conjugated system , amino acid , computational chemistry , stereochemistry , organic chemistry , molecule , biochemistry , physics , astronomy , polymer
Of all the amino acids, the surface of π‐electron conjugated carbon nanoparticles has the largest affinity for tryptophan, followed by tyrosine, phenylalanine, and histidine. In order to increase the binding of a protein to a fullerene, it should suffice to mutate a residue of the site that binds to the fullerene to tryptophan, Trp. Computational chemistry shows that this intuitive approach is fraught with danger. Mutation of a binding residue to Trp may even destabilize the binding because of the complicated balance between van der Waals, polar and non‐polar solvation interactions.