Domain swapping: a mathematical model for quantitative assessment of structural effects.
domain swapping
hydrophobicity
micelle‐like
protein structure
Journal
FEBS open bio
ISSN: 2211-5463
Titre abrégé: FEBS Open Bio
Pays: England
ID NLM: 101580716
Informations de publication
Date de publication:
06 Oct 2024
06 Oct 2024
Historique:
revised:
14
09
2024
received:
30
06
2024
accepted:
27
09
2024
medline:
7
10
2024
pubmed:
7
10
2024
entrez:
6
10
2024
Statut:
aheadofprint
Résumé
The domain-swapping mechanism involves the exchange of structural elements within a secondary or supersecondary structure between two (or more) proteins. The present paper proposes to interpret the domain-swapping mechanism using a model that assesses the structure of proteins (and complexes) based on building the structure of a common hydrophobic core in a micelle-like arrangement (a central hydrophobic core with a polar shell in contact with polar water), which has a considerable impact on the stabilisation of the domain structure built by domain swapping. Domains with a hydrophobicity system that is incompatible with the micelle-like structure have also been identified. This incompatibility is the form of structural codes related to biological function.
Identifiants
pubmed: 39370305
doi: 10.1002/2211-5463.13911
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Uniwersytet Jagielloński Collegium Medicum
ID : N41/DBS/001127
Organisme : European Union's Horizon 2020 Program
ID : 857533
Informations de copyright
© 2024 The Author(s). FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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