Aromatic interactions in peptides: impact on structure and function.
Aromatic interactions, including pi-pi, cation-pi, aryl-sulfur, and carbohydrate-pi interactions, have been shown to be prevalent in proteins through protein structure analysis, suggesting that they are important contributors to protein structure. However, the magnitude and significance of aromatic interactions is not defined by such studies. Investigation of aromatic interactions in the context of structured peptides has complemented studies of protein structure and has provided a wealth of information regarding the role of aromatic interactions in protein structure and function. Recent advances in this area are reviewed.
Waters
Marcey L
ML
Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, NC 27599, USA.
D024322:Amino Acids, Aromatic / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002412:Cations / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism; D008715:Methionine / Q000378:metabolism; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary
D024322:Amino Acids, Aromatic; D002412:Cations; D010455:Peptides; D008715:Methionine; D003545:Cysteine