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1
المؤلفون: Carlo Camilloni, Michele Vendruscolo
المصدر: Journal of the American Chemical Society. 136:8982-8991
مصطلحات موضوعية: Models, Molecular, Protein Denaturation, Work (thermodynamics), Models, Statistical, Chemistry, Metadynamics, Proteins, Energy landscape, General Chemistry, Statistical mechanics, Molecular Dynamics Simulation, Biochemistry, Catalysis, Characterization (materials science), Folding (chemistry), Molecular dynamics, Colloid and Surface Chemistry, Structural biology, Computational chemistry, Acyl Coenzyme A, Statistical physics
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المؤلفون: Guido Tiana, Birthe B. Kragelund, Carlo Camilloni, Immanuel Valpapuram, Ciro Cecconi, Alberto Imparato, Pétur O. Heidarsson, Flemming M. Poulsen
المصدر: Heidarsson, P O, Valpapuram, I, Camilloni, C, Imparato, A, Tiana, G, Poulsen, F M, Kragelund, B B & Cecconi, C 2012, ' A highly compliant protein native state with a spontaneous-like mechanical unfolding pathway ', Journal of American Chemical Society, vol. 134, no. 41, pp. 17068-17075 . https://doi.org/10.1021/ja305862m
Journal of the American Chemical Society
134 (2012): 17068–17075. doi:10.1021/ja305862m
info:cnr-pdr/source/autori:Heidarsson P.O.[ 2 ] ; Valpapuram I.[1]; Camilloni C.[ 4 ]; Imparato A.[ 5 ]; Tiana G.[ 3 ]; Poulsen F.M.[ 2 ] ; Kragelund B.B.[ 2 ]; Cecconi C.[ 1 ]/titolo:A highly compliant protein native state with a spontaneous-like mechanical unfolding pathway/doi:10.1021%2Fja305862m/rivista:Journal of the American Chemical Society (Print)/anno:2012/pagina_da:17068/pagina_a:17075/intervallo_pagine:17068–17075/volume:134مصطلحات موضوعية: Diazepam Binding Inhibitor, Models, Molecular, optical tweezers, Chemistry, General Chemistry, Molecular Dynamics Simulation, protein compliance, Spontaneous-like Mechanical Unfolding, optical tweezers, single molecule studies, Biochemistry, Catalysis, Molten globule, Transition state, Reaction coordinate, Molecular dynamics, Crystallography, Colloid and Surface Chemistry, Optical tweezers, protein compliance, Spontaneous-like Mechanical Unfolding, Helix, Native state, Biophysics, Denaturation (biochemistry), single molecule studies, Protein Unfolding