The denatured state of HIV-1 protease under native conditions

Autor: Guido Tiana, Daniel Malmodin, Birthe B. Kragelund, Alessandro Aliverti, R. A. Broglia, Gregory Potel, Martina Caldarini, Heike I. Rösner, Maria A. Vanoni

Publikováno v: Rösner, H I, Caldarini, M, Potel, G, Malmodin, D, Vanoni, M A, Aliverti, A, Broglia, R A, Kragelund, B B & Tiana, G 2022, ' The denatured state of HIV-1 protease under native conditions ', Proteins: Structure, Function, and Bioinformatics, vol. 90, no. 1, pp. 96-109 . https://doi.org/10.1002/prot.26189

The denatured state of several proteins has been shown to display transient structures that are relevant for folding, stability, and aggregation. To detect them by nuclear magnetic resonance (NMR) spectroscopy, the denatured state must be stabilized

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c6aeab878d94143b012e174cdb4ecae
https://pubmed.ncbi.nlm.nih.gov/34312913

The denatured state of HIV-1 protease under native conditions

Autor: Guido Tiana, Daniel Malmodin, Birthe B. Kragelund, Gregory Potel, R. A. Broglia, Heike I. Rösner, Maria A. Vanoni, Martina Caldarini, Alessandro Aliverti

The denatured state of several proteins has been shown to display transient structures that are relevant for folding, stability and aggregation. To detect them by nuclear magnetic resonance (NMR) spectroscopy, the denatured state must be stabilized b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5db21466a82dbac878f3c4a5db8c5c4c
https://doi.org/10.22541/au.162402688.84511040/v1

The maturation of HIV-1 protease precursor studied by discrete molecular dynamics

Autor: Nikolay V. Dokholyan, Sachie Kimura, Guido Tiana, Martina Caldarini, Ricardo A. Broglia

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 82:633-639

The equilibrium properties of a HIV-1-protease precursor are studied by means of an efficient molecular dynamics scheme, which allows for the simulation of the folding of the protein monomers and their dimerization into an active form and compare the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6d63c94dec1da28cebe1410cb57c0409
https://doi.org/10.1002/prot.24440

The complex folding behavior of HIV-1-protease monomer revealed by optical-tweezer single-molecule experiments and molecular dynamics simulations

Autor: C. Volonté, Guido Tiana, Ricardo A. Broglia, Ciro Cecconi, Maria A. Vanoni, Immanuel Valpapuram, Alessandro Aliverti, Punam Sonar, V. Pandini, Martina Caldarini, Davide Tavella

Publikováno v: Biophysical chemistry
195 (2014): 32–42. doi:10.1016/j.bpc.2014.08.001
info:cnr-pdr/source/autori:Caldarini M. [ 1,2 ] ; Sonar P. [ 3,4 ] ; Valpapuram I. [ 3,4 ] ; Tavella D. [ 1,2 ] ; Volonte C. [ 1,2 ] ; Pandini V. [ 5 ] ; Vanoni M. A. [ 5 ] ; Aliverti A. [ 5 ] ; Broglia R. A. [ 1,2,6 ] ; Tiana G.[ 1,2 ] ; Cecconi C. [ 3,4 ]/titolo:The complex folding behavior of HIV-1-protease monomer revealed by optical-tweezer single-molecule experiments and molecular dynamics simulations/doi:10.1016%2Fj.bpc.2014.08.001/rivista:Biophysical chemistry (Print)/anno:2014/pagina_da:32/pagina_a:42/intervallo_pagine:32–42/volume:195

We have used optical tweezers and molecular dynamics simulations to investigate the unfolding and refolding process of a stable monomeric form of HIV-1-protease (PR). We have characterized the behavior under tension of the native state (. N), and tha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6d4abc8390f2d9fc78c67e43711fc0f
https://pubmed.ncbi.nlm.nih.gov/25194276