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المؤلفون: Carlo Camilloni, Sonia Longhi, Stefano Gianni, Angelo Toto, Francesca Troilo, Maurizio Brunori, Daniela Bonetti
المساهمون: Università degli Studi di Roma 'La Sapienza' [Rome], Department of Biochemical Sciences 'Rossi Fanelli', Institut Pasteur, Fondation Cenci Bolognetti - Istituto Pasteur Italia, Fondazione Cenci Bolognetti, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' [Rome], Dipartimento di Bioscienze [Milano], Università degli studi di Milano [Milano], Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Work was partly supported by grants from the Italian Ministero dell’Istruzione dell’Università e della Ricerca (Progetto di Interesse 'Invecchiamento' to S.G.), Sapienza University of Rome (C26A155S48, B52F16003410005 and RP11715C34AEAC9B to S.G), and the Associazione Italiana per la Ricerca sul Cancro (Individual Grant MFAG 2016, 18701 to S.G.). F.T. is a recipient of a Ph.D. fellowship from the Italo-French University., Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome], Università degli Studi di Milano [Milano] (UNIMI), Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome] (UNIROMA), Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Università degli Studi di Roma 'La Sapienza' = Sapienza University [Rome] (UNIROMA), Università degli Studi di Milano = University of Milan (UNIMI)
المصدر: Journal of Physical Chemistry B
Journal of Physical Chemistry B, American Chemical Society, 2018, 122 (49), pp.11166-11173. ⟨10.1021/acs.jpcb.8b06320⟩
Journal of Physical Chemistry B, 2018, 122 (49), pp.11166-11173. ⟨10.1021/acs.jpcb.8b06320⟩
The journal of physical chemistry. B (1997 : Online) 122 (2018): 11166–11173. doi:10.1021/acs.jpcb.8b06320
info:cnr-pdr/source/autori:Troilo F.; Bonetti D.; Camilloni C.; Toto A.; Longhi S.; Brunori M.; Gianni S./titolo:Folding Mechanism of the SH3 Domain from Grb2/doi:10.1021%2Facs.jpcb.8b06320/rivista:The journal of physical chemistry. B (1997 : Online)/anno:2018/pagina_da:11166/pagina_a:11173/intervallo_pagine:11166–11173/volume:122مصطلحات موضوعية: folding, 0301 basic medicine, 030103 biophysics, Protein Conformation, kinetic, GAB2, macromolecular substances, Molecular Dynamics Simulation, Antiparallel (biochemistry), SH3 domain, src Homology Domains, 03 medical and health sciences, Molecular dynamics, Escherichia coli, Materials Chemistry, Humans, Amino Acid Sequence, transition state, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Physical and Theoretical Chemistry, GRB2 Adaptor Protein, Protein Unfolding, chemistry.chemical_classification, biology, Protein tertiary structure, Surfaces, Coatings and Films, Amino acid, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], Kinetics, 030104 developmental biology, chemistry, Mutation, Mutagenesis, Site-Directed, biology.protein, Biophysics, GRB2, Target protein, Sequence Alignment
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المؤلفون: Carlo Camilloni, Thomas Löhr, Alexander Jussupow
المصدر: The Journal of chemical physics. 146(16)
مصطلحات موضوعية: 0301 basic medicine, Physics::Biological Physics, Quantitative Biology::Biomolecules, 010304 chemical physics, Chemistry, Protein Conformation, Metadynamics, General Physics and Astronomy, Bayes Theorem, Molecular Dynamics Simulation, 01 natural sciences, Force field (chemistry), Weighting, 03 medical and health sciences, 030104 developmental biology, Models, Chemical, Computational chemistry, 0103 physical sciences, Statistical physics, Amino Acid Sequence, Physical and Theoretical Chemistry, Peptides, Nuclear Magnetic Resonance, Biomolecular, Oligopeptides