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Dynamics and unfolding pathway of chimeric azurin variants: insights from molecular dynamics simulation.

Autor: Evoli, Stefania, Guzzi, Rita, Rizzuti, Bruno¹ bruno.rizzuti@cnr.it

Publikováno v: Journal of Biological Inorganic Chemistry (JBIC). Oct2013, Vol. 18 Issue 7, p739-749. 11p.

Molecular simulations of beta-lactoglobulin complexed with fatty acids reveal the structural basis of ligand affinity to internal and possible external binding sites

Autor: Evoli, Stefania, Guzzi, Rita, Rizzuti, Bruno

Publikováno v: Proteins
82 (2014): 2609–2619. doi:10.1002/prot.24625
info:cnr-pdr/source/autori:Evoli, Stefania; Guzzi, Rita; Rizzuti, Bruno/titolo:Molecular simulations of beta-lactoglobulin complexed with fatty acids reveal the structural basis of ligand affinity to internal and possible external binding sites/doi:10.1002%2Fprot.24625/rivista:Proteins (Print)/anno:2014/pagina_da:2609/pagina_a:2619/intervallo_pagine:2609–2619/volume:82

The interaction of saturated fatty acids of different length (C8:0 to C18:0) with beta-lactoglobulin (beta LG) was investigated by molecular dynamics simulation and docking approaches. The results show that the presence of such ligands in the hydroph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::2f015847db66f432f1a44da369a1ded4

Molecular simulations of β-lactoglobulin complexed with fatty acids reveal the structural basis of ligand affinity to internal and possible external binding sites.

Autor: Evoli, Stefania, Guzzi, Rita, Rizzuti, Bruno

Publikováno v: Proteins; Oct2014, Vol. 82 Issue 10, p2609-2619, 11p

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