Premium
Interactions between hydrophobic side chains within α‐helices
Author(s) -
Creamer Trevor P.,
Rose George D.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040706
Subject(s) - side chain , helix (gastropod) , chemistry , pairwise comparison , residue (chemistry) , stereochemistry , hydrophobic effect , crystallography , computational chemistry , mathematics , biochemistry , biology , organic chemistry , ecology , statistics , snail , polymer
The thermodynamic basis of helix stability in peptides and proteins is a topic of considerable interest. Accordingly, we have computed the interactions between side chains of all hydrophobic residue pairs and selected triples in a model helix, using Boltzmann‐weighted exhaustive modeling. Specifically, all possible pairs from the set Ala, Cys, His, Ile, Leu, Met, Phe, Trp, Tyr, and Val were modeled at spacings of ( i, i + 2), ( i, i + 3), and ( i, i + 4) in the central turn of a model poly‐alanyl α‐helix. Significant interactions —both stabilizing and destabilizing —were found to occur at spacings of ( i, i + 3) and ( i, i + 4), particularly in side chains with rings (i.e., Phe, Tyr, Trp, and His). In addition, modeling of leucine triples in a helix showed that the free energy can exceed the sum of pairwise interactions in certain cases. Our calculated interaction values both rationalize recent experimental data and provide previously unavailable estimates of the constituent energies and entropies of interaction.