Výsledky vyhledávání - "Avijeet Kulshrestha"

Cholesterol catalyzes unfolding in membrane inserted motifs of the pore forming protein cytolysin A

Autor: Avijeet Kulshrestha, Sudeep N Punnathanam, Rahul Roy, K Ganapathy Ayappa

Plasma membrane induced protein folding and conformational transitions play a central role in cellular homeostasis. Several transmembrane proteins are folded in the complex lipid milieu to acquire a specific structure and function. Bacterial pore for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2c004950affd67480ff2006051c68d72
https://doi.org/10.1101/2023.05.07.539733

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Conformational Flexibility Is a Key Determinant for the Lytic Activity of the Pore-Forming Protein, Cytolysin A

Autor: Avijeet Kulshrestha, Satyaghosh Maurya, Twinkle Gupta, Rahul Roy, Sudeep N Punnathanam, K. Ganapathy Ayappa

Publikováno v: The journal of physical chemistry. B.

Several bacterial infections are mediated by pore-forming toxins (PFTs), a subclass of proteins that oligomerize on mammalian cell membranes forming lytic nanopores. Cytolysin A (ClyA), an α-PFT, undergoes a dramatic conformational change restructur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af60a47169e80b74273c735512f25d55
https://pubmed.ncbi.nlm.nih.gov/36542809

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Finite temperature string method with umbrella sampling using path collective variables: application to secondary structure change in a protein

Autor: Avijeet Kulshrestha, Sudeep N. Punnathanam, K. Ganapathy Ayappa

Publikováno v: Soft matter. 18(39)

The transition of an α-helix to a β-sheet in proteins is among the most complex conformational changes seen in biomolecular systems. Due to long time scales involved in the transition, it is challenging to study such protein conformational changes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a7dbac1d9716e705122f4ab8bbdf49e
https://pubmed.ncbi.nlm.nih.gov/36165347

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Computing the mechanism of α-helix to β-sheet transition in proteins using the finite temperature string method

Autor: Avijeet Kulshrestha, Sudeep N Punnathanam, K Ganapathy Ayappa

The transition of an α-helix to a β-sheet in proteins is among the most complex conformational changes seen in bio-molecular systems. Currently, it is difficult to study such protein conformational changes in a direct molecular dynamics simulation.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::626a024996305f671520d05c081a78a7
https://doi.org/10.1101/2022.07.21.500930

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Conformational flexibility is a key determinant of the lytic activity of the pore forming protein, Cytolysin A

Autor: K. Ganapathy Ayappa, Satyaghosh Maurya, Rahul Roy, Avijeet Kulshrestha, Twinkle Gupta, Sudeep N. Punnathanam

Bacterial pore-forming toxins (PFTs) bind and oligomerize on mammalian cell membranes forming nanopores, that cause cell lysis to promote a wide range of bacterial infections. Cytolysin A (ClyA), an alpha(α)-PFT, is known to undergo one of the large

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41746be165c89f3ecac677f678a3cd82
https://doi.org/10.1101/2021.10.23.465544

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