Premium
Structure‐based analysis of thermodynamic and mechanical properties of cavity‐containing proteins – case study of plant pathogenesis‐related proteins of class 10
Author(s) -
Chwastyk Mateusz,
Jaskolski Mariusz,
Cieplak Marek
Publication year - 2014
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12611
Subject(s) - folding (dsp implementation) , protein folding , pathogenesis , crystallography , chemistry , biophysics , biological system , chemical physics , physics , materials science , biology , biochemistry , engineering , immunology , electrical engineering
We provide theoretical comparisons of the physical properties of eighteen proteins with the pathogenesis‐related proteins of class 10 ( PR ‐10) fold, which is characterized by a large hydrophobic cavity enclosed between a curved β‐sheet and a variable α‐helix. Our novel algorithm to calculate the volume of internal cavities within protein structures is used to demonstrate that, although the sizes of the cavities of the investigated PR ‐10 proteins vary significantly, their other physical properties, such as thermodynamic and mechanical parameters or parameters related to folding, are very close. The largest variations (in the order of 20%) are predicted for the optimal folding times. We show that, on squeezing, the PR ‐10 proteins behave differently from typical virus capsids.