Literature DB >> 15478139

Aromatic interactions in peptides: impact on structure and function.

Marcey L Waters1.   

Abstract

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. (c) 2004 Wiley Periodicals, Inc.

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Year:  2004        PMID: 15478139     DOI: 10.1002/bip.20144

Source DB:  PubMed          Journal:  Biopolymers        ISSN: 0006-3525            Impact factor:   2.505


  27 in total

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9.  Environmentally responsive histidine-carboxylate zipper formation between proteins and nanoparticles.

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10.  A multi-species comparative structural bioinformatics analysis of inherited mutations in alpha-D-mannosidase reveals strong genotype-phenotype correlation.

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