Publicaciones en colaboración con investigadores/as de Universidad de Almería (5)

2020

  1. Human importin α3 and its N-terminal truncated form, without the importin-β-binding domain, are oligomeric species with a low conformational stability in solution

    Biochimica et Biophysica Acta - General Subjects, Vol. 1864, Núm. 7

2016

  1. The Monomeric Species of the Regulatory Domain of Tyrosine Hydroxylase Has a Low Conformational Stability

    Biochemistry, Vol. 55, Núm. 24, pp. 3418-3431

2011

  1. The conformational stability and biophysical properties of the eukaryotic thioredoxins of Pisum sativum are not family-conserved

    PLoS ONE, Vol. 6, Núm. 2

2010

  1. The N-terminal domain of the enzyme I is a monomeric well-folded protein with a low conformational stability and residual structure in the unfolded state

    Protein Engineering, Design and Selection, Vol. 23, Núm. 9, pp. 729-742

2008

  1. The family 52 β-xylosidase from Geobacillus stearothermophilus is a dimer: Structural and biophysical characterization of a glycoside hydrolase

    Biochimica et Biophysica Acta - Proteins and Proteomics, Vol. 1784, Núm. 12, pp. 1924-1934