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Environment of Tryptophan Side Chains in Proteins by Uttamkumar Samanta; Debnath Pal; Pinak Chakrabarti is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Environment of Tryptophan Side Chains in Proteins about?

Although relatively rare, the tryptophan residue (Trp), with its large hydrophobic surface, has a unique role in the folded structure and the binding site of many proteins, and its fluorescence properties make it very useful in studying the structures and dynamics of protein molecules in solution. An analysis has been made of its environment and the geometry of its interaction with neighbors using 719 Trp residues in 180 different protein structures. The distribution of the number of partners interacting with the Trp aromatic ring shows a peak at 6 (considering protein residues only) and 8 (including water and substrate molecules also). The means of the solvent-accessible surface areas of the ring show an exponential decrease with the increase in the number of partners; this relationship can be used to assess the efficiency of packing of residues around Trp. Various residues exhibit different propensities of binding the Trp side chain. The aromatic residues, Met and Pro have high values, whereas the smaller and polar-chain residues have weaker propensities. Most of the interactions are with residues far away in sequence, indicating the importance of Trp in stabilizing the tertiary

Who reads Environment of Tryptophan Side Chains in Proteins?

Author

Uttamkumar Samanta; Debnath Pal; Pinak Chakrabarti

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2000

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)