Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles.

doi:10.1016/0022-2836(91)90725-l

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Article

Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles.

Journal of molecular biology - 20 Mar 1991

Serrano L, Bycroft M, Fersht A R

Abstract excerpt

The side-chains of phenylalanine and tyrosine residues in proteins are frequently found to be involved in pairwise interactions. These occur both within repeating elements of secondary structure and in tertiary and quaternary interactions. It has been suggested that they are important in protein folding and stability, and non-bonded potential energy calculations indicate that a typical aromatic-aromatic...

Topics

Amino Acid Sequence
Bacillus
Bacterial Proteins
Base Sequence
DNA
Enzyme Stability
Hydrocarbons
Hydrogen Bonding
Magnetic Resonance Spectroscopy
Mathematics
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phenols

Phenylalanine

Protein Denaturation

Ribonucleases

Thermodynamics

Tyrosine

Source

Open in PubMed

Identifiers

PMID: 2010920
DOI: 10.1016/0022-2836(91)90725-l

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2010920-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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