Browsing Institute of Advanced Materials (INAM) by Author "37a9f07e-beab-42c6-94e1-4edad7eb11b1"
Now showing items 1-4 of 4
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Activation and friction in enzymatic loop opening and closing dynamics
Zinovjev, Kirill; Guénon, Paul; Ramos Guzmán, Carlos Alberto; Ruiz-Pernía, José Javier; Laage, Damien; Tuñón, Iñaki Springer Nature (2024-03-20)Protein loop dynamics have recently been recognized as central to enzymatic activity, specificity and stability. However, the factors controlling loop opening and closing kinetics have remained elusive. Here, we combine ... -
Elucidation of the Active Form and Reaction Mechanism in Human Asparaginase Type III Using Multiscale Simulations
Anđelković, Milorad; Zinovjev, Kirill; Ramos Guzmán, Carlos Alberto; Ruiz-Pernía, José Javier; Tuñón, Iñaki American Chemical Society (2023-08-27)l-asparaginases catalyze the asparagine hydrolysis to aspartate. These enzymes play an important role in the treatment of acute lymphoblastic leukemia because these cells are unable to produce their own asparagine. Due to ... -
The impact of SARS-CoV-2 3CL protease mutations on nirmatrelvir inhibitory efficiency. Computational insights into potential resistance mechanisms
Ramos Guzmán, Carlos Alberto; Anđelković, Milorad; Zinovjev, Kirill; Ruiz-Pernía, José Javier; Tuñón, Iñaki The Royal Society of Chemistry (2023-02-14)The use of antiviral drugs can promote the appearance of mutations in the target protein that increase the resistance of the virus to the treatment. This is also the case of nirmatrelvir, a covalent inhibitor of the 3CL ... -
Unveiling the Mechanistic Singularities of Caspases: A Computational Analysis of the Reaction Mechanism in Human Caspase-1
Ramos Guzmán, Carlos Alberto; Ruiz-Pernía, José Javier; Zinovjev, Kirill; Tuñón, Iñaki American Chemical Society (2023-04-07)Caspases are cysteine proteases in charge of breaking a peptide bond next to an aspartate residue. Caspases constitute an important family of enzymes involved in cell death and inflammatory processes. A plethora of diseases, ...