| Autor: |
Williams, Lawrence J., Schendt, Brian J., Fritz, Zachary R., Attali, Yonatan, Lavroff, Robert H., Yarmush, Martin L. |
| Předmět: |
|
| Zdroj: |
TECHNOLOGY; Mar-Jun2019, Vol. 7 Issue 1/2, p12-39, 28p |
| Abstrakt: |
Here we present a model to estimate the interaction free energy contribution of each amino acid residue of a given protein. Protein interaction energy is described in terms of per-residue interaction factors, μ. Multibody interactions are implicitly captured in μ through the combination of amino acid terms (γ) guided by local conformation indices (σ). The model enables construction of an interaction factor heat map for a protein in a given fold, allows prima facie assessment of the degree of residue–residue interaction, and facilitates a qualitative and quantitative evaluation of protein association properties. The model was used to compute thermal stability of T4 bacteriophage lysozyme mutants across seven sites. Qualitative assessment of mutational effects provides a straightforward rationale regarding whether a particular site primarily perturbs native or non-native states, or both. The presented model was found to be in good agreement with experimental mutational data ( R 2 = 0. 7 3) and suggests an approach by which to convert structure space into energy space. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
