Zobrazeno 1 - 10
of 120
pro vyhledávání: '"Krzysztof Kuczera"'
Publikováno v:
Crystals, Vol 14, Iss 6, p 532 (2024)
We present an analysis of α-helix folding in the coarse-grained coordinate of number of formed helical hydrogen bonds (NHBs) for four alanine peptides (ALA)n, with n = 5, 8, 15, and 21 residues. Starting with multi-microsecond all-atom molecular dyn
Externí odkaz:
https://doaj.org/article/078c5591d3d04fc7887aa01d7f69df7c
Autor:
Alex A. Meier, Hee-Jung Moon, Ronald Toth, Ewa Folta-Stogniew, Krzysztof Kuczera, C. Russell Middaugh, Minae Mure
Publikováno v:
Biomolecules, Vol 11, Iss 12, p 1846 (2021)
Lysyl oxidase-like 2 (LOXL2) has emerged as a promising therapeutic target against metastatic/invasive tumors and organ and tissue fibrosis. LOXL2 catalyzes the oxidative deamination of lysine and hydroxylysine residues in extracellular matrix (ECM)
Externí odkaz:
https://doaj.org/article/8ff12db5c7694f44b9580dd423ef49a8
Publikováno v:
Biomolecules, Vol 11, Iss 9, p 1351 (2021)
Fast kinetic experiments with dramatically improved time resolution have contributed significantly to understanding the fundamental processes in protein folding pathways involving the formation of a-helices and b-hairpin, contact formation, and overa
Externí odkaz:
https://doaj.org/article/34871284919c4217ae02b01cb7ce2dad
Publikováno v:
Life, Vol 11, Iss 5, p 385 (2021)
We present a computer simulation study of helix folding in alanine homopeptides (ALA)n of length n = 5, 8, 15, and 21 residues. Based on multi-microsecond molecular dynamics simulations at room temperature, we found helix populations and relaxation t
Externí odkaz:
https://doaj.org/article/79ee655d5c9049c69cca681d76abbee8
Publikováno v:
The Journal of Physical Chemistry B. 126:2647-2657
The ability of phytochromes to act as photoswitches in plants and microorganisms depends on interactions between a bilin-like chromophore and a host protein. The interconversion occurs between the spectrally distinct red (Pr) and far-red (Pfr) confor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::283859edb39fd8d58399c46e5f67fab1
https://doi.org/10.1021/acs.jpcb.2c00131
https://doi.org/10.1021/acs.jpcb.2c00131
Autor:
Kyung-Hoon, Lee, Krzysztof, Kuczera
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 41:2619-2629
Prion diseases are neurodegenerative disorders caused by spongiform degeneration of the brain. Understanding the fundamental mechanism of prion protein aggregation caused by mutations is very crucial to resolve the pathology of prion diseases. To hel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8bcf6097fb9c47a2dcf6a40816a477c
https://doi.org/10.1080/07391102.2022.2036237
https://doi.org/10.1080/07391102.2022.2036237
We have performed molecular dynamics (MD) and replica-exchange (REMD) simulations of folding of the GB1 hairpin peptide in aqueous solution. REMD results were consistent with a cooperative zipper folding model. 120 μs MD trajectories at 320 K yielde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::992cf19c27478d99dc30a2c88440be92
Publikováno v:
The Journal of Physical Chemistry B. 125:10972-10984
Picosecond time-resolved fluorescence anisotropy was used to measure the effect of denaturants and osmolytes on the reorientation dynamics of the simplest dipeptide. The solvent denaturants guanidinium hydrochloride (gdm), urea, and the osmolyte prol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d0afc724e9495a3e18f691db43418f2
https://doi.org/10.1021/acs.jpcb.1c06838
https://doi.org/10.1021/acs.jpcb.1c06838
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 21; Pages: 13385
Lysyl oxidase–like 2 (LOXL2) has been recognized as an attractive drug target for anti–fibrotic and anti–tumor therapies. However, the structure–based drug design of LOXL2 has been very challenging due to the lack of structural information of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7df6df249a122afeafb557aeab802300
Publikováno v:
The journal of physical chemistry. B. 126(44)
In this paper we derive analytically from molecular dynamics (MD) simulations the friction coefficients related to conformational transitions within several model peptides with α-helical structures. We study a series of alanine peptides with various
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cc5e16ee29303b20636ca37ef476c2b
https://pubmed.ncbi.nlm.nih.gov/36300354
https://pubmed.ncbi.nlm.nih.gov/36300354