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Updated: May 10, 2026

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis
Published on: October 15, 2019
Hydrophobic core formation in protein complex of cathepsin
Monika Piwowar1, Mateusz Banach, Leszek Konieczny
1a Department of Bioinformatics and Telemedicine , Medical College - Jagiellonian University , Lazarza 16 , 31-530 , Krakow , Poland .
Abstract:
The "fuzzy oil drop" model assumes that the idealized hydrophobic core in a protein body can be described by a 3D Gauss function. The structure of the 1ICF protein (cathepsin), which participates in the proteolysis process and has cysteine-type peptidase activity, has been analyzed on the basis of the "fuzzy oil drop" model. The authors have determined the contribution of individual exon fragments to the creation of a common hydrophobic core and assessed the involvement of each chain in this process, depending on the number of complexed chains. Quantitative assessment of exons, chains, dimers, and the whole complex suggest that each of these units plays a different role in shaping the protein's hydrophobic core.
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