Εξειδίκευση τύπου :	Άρθρο σε επιστημονικό περιοδικό
Τίτλος:	Structure of amino acid sequence-reversed wtRop protei: insights from atomistic molecular dynamics simulations
Δημιουργός/Συγγραφέας:	Arnittali, Maria [EL] Ρισσάνου, Αναστασία[EN] Rissanou, Anastassia Kefala, Aikaterini Kokkinidis, Michael Harmandaris, Vagelis
Ημερομηνία:	2023-09-06
Γλώσσα:	Αγγλικά
ISSN:	0739-1102 1538-0254
DOI:	10.1080/07391102.2023.2252903
Άλλο:	37671833
Περίληψη:	This study aims to the investigation of the advantages of designing new proteins presume upon a 'bias' sequence of amino acids, based on the reversed sequence of parent proteins, such as the retro ones. The structural simplicity of wtRop offers a very attractive model system to study these aspects. The current work is based on all-atom Molecular Dynamics (MD) simulations and corresponding experimental evidence on two different types of reversed wtRop protein, one with a fully reversed sequence of amino acids (rRop) and another with a partially reversed sequence (prRop), where only the five residues of the loop region (30ASP-34GLN) were not reversed. The exploration of the structure of the two retro proteins is performed highlighting the similarities and the differences with their parent protein, by employing various measures. Two models have been studied for both reversed proteins, a dimeric and a monomeric with the former one found to be more stable than the latter. Preferable equilibrium structures that the protein molecule can attain are explored, indicating the equilibration pathway. Simulation findings indicate a disruption of the α-helical structure and the appearance of additional secondary structures for both retro proteins. Reduced structural stability compared to their parent protein (wtRop) is also found. A corruption of the hydrophobic core is observed in the dimeric models. Furthermore, the simulations findings are consistent with the experimental characterization of prRop by circular dichroism spectroscopy (CD) which highlights an unstable, highly α-helical protein.Communicated by Ramaswamy H. Sarma.
Τίτλος πηγής δημοσίευσης:	Journal of biomolecular structure & dynamics
Θεματική Κατηγορία:	[EL] Βιοχημεία[EN] Biochemistry
Λέξεις-Κλειδιά:	Retro proteins Heptad pattern Molecular dynamics Protein folding Secondary structure Amino acid sequence Heptad pattern
EU Grant:	Molecular Simulations and Free Energy Calculations of Proteins, MDMET OH-C project
Κάτοχος πνευματικών δικαιωμάτων:	© 2023 Informa UK Limited, trading as Taylor & Francis Group.
Ηλεκτρονική διεύθυνση στον εκδότη (link):	https://doi.org/10.1080/07391102.2023.2252903
Εμφανίζεται στις συλλογές:	Ινστιτούτο Θεωρητικής και Φυσικής Χημείας (ΙΘΦΧ) - Επιστημονικό έργο