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• Infrared Spectroscopy Structural Studies of Biomolecules

• Exploring polar headgroup interactions between sphingomyelin and ceramide with infrared spectroscopy

  de la Arada I, González-Ramírez EJ, Alonso A, Goñi FM, Arrondo JR.

  Sci Rep. 10(1):17606. (2020) doi: 10.1038/s41598-020-74781-8. (2020)

• Conjugative Coupling Proteins and the Role of Their Domains in Conjugation, Secondary Structure and in vivo Subcellular Location

  Álvarez-Rodríguez I, Ugarte-Uribe B, de la Arada I, Arrondo JLR, Garbisu C, Alkorta I.

  Front Mol Biosci. 7:185. (2020) doi: 10.3389/fmolb.2020.00185. (2020)

• Cholesterol Constrains the Antigenic Configuration of the Membrane-Proximal Neutralizing HIV-1 Epitope

  Torralba J, de la Arada I, Carravilla P, Insausti S, Rujas E, Largo E, Eggeling C, Arrondo JLR, Apellániz B, Nieva JL.

  ACS Infect Dis. 6(8):2155-2168. (2020) doi: 10.1021/acsinfecdis.0c00243 (2020)

• The Binding of Aβ42 Peptide Monomers to Sphingomyelin/Cholesterol/Ganglioside Bilayers Assayed by Density Gradient Ultracentrifugation

  Ahyayauch H, de la Arada I, Masserini ME, Arrondo JLR, Goñi FM, Alonso A.

  Int J Mol Sci. 21(5). pii: E1674. (2020) doi: 10.3390/ijms21051674. (2020)

• Molecular Characterization of the Viroporin Function of Foot-and-Mouth Disease Virus Nonstructural Protein 2B

  DP Gladue, E Largo, I de la Arada, VM Aguilella, A Alcaraz, JLR Arrondo, LG Holinka, E Brocchi, E Ramirez-Medina, EA Vuono, KA Berggren, C Carrillo, JL Nieva, MV Borca.

  J Virol. 92(23). pii: e01360-18. doi: 10.1128/JVI.01360-18. (2018)

• 2D IR Correlation Spectroscopy in the Determination of Aggregation and Stability of KH Domain GXXG Loop Peptide in the Presence and Absence of Trifluoroacetate

  A.R. Nassif, I. de la Arada, J.L. Arrondo and B. Pastrana-Rios

  Anal Chem 89, 5766-5776 doi: 10.1021/acs.analchem.6b04800 (2017)

• The conformation of human phospholipid scramblase 1, as studied by infrared spectroscopy. Effects of calcium and detergent

  N. Andraka, L. Sanchez-Magraner, M. Garcia-Pacios, F.M. Goni and J.L.R. Arrondo

  Biochim Biophys Acta 1859, 1019-1028 doi: 10.1016/j.bbamem.2017.02.015 (2017)

• Structural changes induced by acidic pH in human apolipoprotein B-100

  J.A. Fernández-Higuero, A. Benito-Vicente, A. Etxebarria, J.C. Milicua, H. Ostolaza, J.L. Arrondo and C. Martín

  Sci Rep. 6, 36324 doi: 10.1038/srep36324 (2016)

• Solid lipid nanoparticles for delivery of Calendula officinalis extract

  Arana L, Salado C, Vega S, Aizpurua-Olaizola O, Arada I, Suarez T, Usobiaga A, Arrondo JL, Alonso A, Goni FM, Alkorta I

  Colloid Surface B. 135:18-26 (2015)

• Human LDL structural diversity studied by IR spectroscopy.

  J.A. Fernández-Higuero, A.M. Salvador, C. Martín, J.C. Milicua and J.L. Arrondo.

  PLoS One 9, e92426 (2014).

• The C-terminal transmembrane domain of human phospholipid scramblase 1 is essential for the protein flip-flop activity and Ca2+-binding.

  L. Sánchez-Magraner, I.M. Posada, N. Andraka, F.X. Contreras, A.R. Viguera, D.M. Guérin, J.L.R. Arrondo, H.L. Monaco and F.M. Goñi.

  J Membr Biol. 247, 155-165 (2014).

• Structure and immunogenicity of a peptide vaccine, including the complete HIV-1 gp41 2F5 epitope: implications for antibody recognition mechanism and immunogen design.

  S. Serrano, A. Araujo, B. Apellániz, S. Bryson, P. Carravilla, I. de la Arada, N. Huarte, E. Rujas, E.F. Pai, J.L.R. Arrondo, C. Domene, M.A. Jiménez and J.L. Nieva.

  J Biol Chem. 289, 6565-6580 (2014).

• Deletion of a single helix from the transmembrane domain causes large changes in membrane insertion properties and secondary structure of the bacterial conjugation protein TrwB

  A.J. Vecino, R. de L. Segura, I. de la Arada, F. de la Cruz, F.M. Goñi, J.L. Arrondo and I. Alkorta.

  Biochim Biophys Acta. 1818, 3158-3166 (2012).

• Binding of b-Amyloid (1–42) peptide to negatively charged phospholipid membranes in the liquid-ordered state: modeling and experimental studies.

  H. Ahyayauch, M. Raab, J.V. Busto, N. Andraka, J.L. R. Arrondo, M. Masserini, I. Tvaroska and F.M. Goñi.

  Biophys. J. 103, 453–463 (2012).

• Model systems of precursor cellular membranes: long-chain alcohols stabilize spontaneously formed oleic acid vesicles.

  A. Rendón, D. Gil Carton, J. Sot, M. García-Pacios, L.R. Montes, M. Valle, J.L.R. Arrondo, F.M. Goñi and K. Ruiz-Mirazo

  Biophys. J. 102, 278–286 (2012).

• A conventional and 2DCOS infrared approach to the kinetics of protein misfolding.

  I. de la Arada, N. Andraka, M. Garcia Pacios and J.L.R. Arrondo.

  Current Protein & Peptide Science 12, 181-187 (2011).

• Membrane insertion stabilizes the structure of TrwB, the R388 conjugative plasmid coupling protein.

  A.J. Vecino, I. de la Arada, R.L. Segura, F.M. Goñi, F. de Cruz, J.L. R. Arrondo and I. Alkorta.

  Biochim. Biophys. Acta 1808, 1032-1039 (2011).