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Biochemistry ; 60(26): 2064-2070, 2021 07 06.
Article in English | MEDLINE | ID: mdl-34137579

ABSTRACT

Here we show that an NH-π interaction between a highly conserved Asn and a nearby Trp stabilizes the WW domain of the human protein Pin1. The strength of this NH-π interaction depends on the structure of the arene, with NH-π interactions involving Trp or naphthylalanine being substantially more stabilizing than those involving Tyr or Phe. Calculations suggest arene size and polarizability are key structural determinants of NH-π interaction strength. Methylation or PEGylation of the Asn side-chain amide nitrogen each strengthens the associated NH-π interaction, though likely for different reasons. We hypothesize that methylation introduces steric clashes that destabilize conformations in which the NH-π interaction is not possible, whereas PEGylation strengthens the NH-π interaction via localized desolvation of the protein surface.


Subject(s)
Asparagine/chemistry , Hydrogen Bonding/drug effects , NIMA-Interacting Peptidylprolyl Isomerase/chemistry , Polyethylene Glycols/chemistry , Tryptophan/chemistry , WW Domains/drug effects , Amino Acid Sequence , Humans , Methylation , Models, Molecular , Mutation , NIMA-Interacting Peptidylprolyl Isomerase/genetics , Protein Conformation , Thermodynamics , WW Domains/genetics
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