A new route for the determination of protein structure and function

Understanding complex biological macromolecules, especially proteins, is vital for grasping their diverse chemical functions with direct impact on biology and pharmacology. Techniques such as x-ray crystallography and cryo-electron microscopy face limitations such as radiation damage and difficulties in crystallizing certain proteins. To address this, we present a strategic concept involving engineered protein scaffolds to create ordered arrays of proteins with controlled orientations, aiming at enhancing the signal at the detector. This innovative strategy opens avenues to solve the existing challenges for determining protein structures under physiological conditions. Moreover, it holds promise for studying conformational changes resulting from photoinduced changes, protein–drug, and/or protein–protein interactions. In the near future, our group will focus on showing the potential of the proposed strategy by combining molecular biology, protein self-assembly, and x-ray spectroscopy.

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Publication Details

Journal
AIP Advances
Published
2025-08-01
DOI
https://doi.org/10.1063/5.0214579
Primary Topic
Enzyme Structure and Function
Type
article
Field-Weighted Citation Impact
0.00

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article

A new route for the determination of protein structure and function

Aitziber L. Cortajarena, Cristian Svetina, Angelo Beratto-Ramos, Riccardo Mincigrucci et al.
AIP Advances
Enzyme Structure and Function
article

A new route for the determination of protein structure and function

Aitziber L. Cortajarena, Cristian Svetina, Angelo Beratto-Ramos, Riccardo Mincigrucci, Sara H. Mejías, C. Masciovecchio
article en

Abstract

Understanding complex biological macromolecules, especially proteins, is vital for grasping their diverse chemical functions with direct impact on biology and pharmacology. Techniques such as x-ray crystallography and cryo-electron microscopy face limitations such as radiation damage and difficulties in crystallizing certain proteins. To address this, we present a strategic concept involving engineered protein scaffolds to create ordered arrays of proteins with controlled orientations, aiming at enhancing the signal at the detector. This innovative strategy opens avenues to solve the existing challenges for determining protein structures under physiological conditions. Moreover, it holds promise for studying conformational changes resulting from photoinduced changes, protein–drug, and/or protein–protein interactions. In the near future, our group will focus on showing the potential of the proposed strategy by combining molecular biology, protein self-assembly, and x-ray spectroscopy.

AIP AdvancesVol. 15(8)
Madrid Institute for Advanced Studies (ES), Ikerbasque (ES), IMDEA Nanoscience (ES), Elettra-Sincrotrone Trieste S.C.p.A. (IT), CIC biomaGUNE (ES), Centro Nacional de Biotecnología (ES), European X-Ray Free-Electron Laser (DE)
Fundación BBVA, “la Caixa” Foundation, Ministerio de Ciencia e Innovación, Banco Bilbao Vizcaya Argentaria, Fundación Bancaria Caixa d'Estalvis i Pensions de Barcelona, Agencia Estatal de Investigación
Openalex Percentile: Top 86%
Enzyme Structure and Function
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A new route for the determination of protein structure and function — Aitziber L. Cortajarena, Cristian Svetina, et al. · AIP Advances (2025) | TGRS Research Map | TGRS