Raúl Pérez‐Jiménez

ORCID: 0000-0001-7094-6799
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About
Contact & Profiles
Research Areas
  • Force Microscopy Techniques and Applications
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Mechanical and Optical Resonators
  • RNA and protein synthesis mechanisms
  • Redox biology and oxidative stress
  • Advanced Electron Microscopy Techniques and Applications
  • Biochemical and Structural Characterization
  • Cellular Mechanics and Interactions
  • Biofuel production and bioconversion
  • CRISPR and Genetic Engineering
  • Cardiomyopathy and Myosin Studies
  • Monoclonal and Polyclonal Antibodies Research
  • Advanced Fluorescence Microscopy Techniques
  • Advanced Cellulose Research Studies
  • Enzyme Production and Characterization
  • thermodynamics and calorimetric analyses
  • Ion channel regulation and function
  • Lipid Membrane Structure and Behavior
  • Muscle Physiology and Disorders
  • Molecular Junctions and Nanostructures
  • Heat shock proteins research
  • Organometallic Compounds Synthesis and Characterization
  • Hemoglobin structure and function
  • Spectroscopy and Quantum Chemical Studies

CIC bioGUNE
2023-2025

Ikerbasque
2015-2025

Euskadiko Parke Teknologikoa
2025

CIC nanoGUNE
2014-2022

University of the Basque Country
2022

Columbia University
2006-2013

Universidad de Granada
2004-2011

University of Maryland, College Park
2005-2010

Consejo Superior de Investigaciones Científicas
2009-2010

Centro de Investigaciones Biológicas Margarita Salas
2009-2010

The molecular mechanism by which a mechanical stimulus is translated into chemical response in biological systems still unclear. We show that stretching of single cytoplasmic proteins can activate binding other molecules. used magnetic tweezers, total internal reflection fluorescence, and atomic force microscopy to investigate the effect on interaction between talin, protein links liganded membrane integrins cytoskeleton, vinculin, focal adhesion activated talin binding, leading...

10.1126/science.1162912 article EN Science 2009-01-29

Alginate and nanocellulose are potential biomaterials to be employed as bioinks for three-dimensional (3D) printing. Alginate-cellulose nanofibers (A-CNF) formulations with CNF amounts up 5 wt% were developed rheologically characterized evaluate their printability. Results showed that less than 3 did not present suitable characteristics ensure shape fidelity after Selected A-CNF 3D printed freeze-dried obtain porous scaffolds. Morphological mechanical analysis performed, showing contributed...

10.1016/j.carbpol.2021.118026 article EN cc-by-nc-nd Carbohydrate Polymers 2021-04-02

Abstract Improving the efficiency of enzymes towards decomposing substrates has been one central goals in biotechnology industry. However, modification for upgrading natural materials to high-value performant is largely unexplored. Here, we demonstrate that ancestral form a Cel5A bacterial endoglucanase, unlike its modern descendant from Bacillus subtilis , was able generate cellulose nanocrystals (EnCNC) chemically pure, maintaining native structure and displaying higher thermal stability...

10.1038/s43246-020-00055-5 article EN cc-by Communications Materials 2020-08-12

Abstract Uropathogenic Escherichia coli attach to tissues using pili type 1. Each pilus is composed by thousands of coiled FimA domains followed the tip fibrillum, FimF-FimG-FimH. The are linked non-covalent β-strands that must resist mechanical forces during attachment. Here, we use single-molecule force spectroscopy measure contribution each domain stability and monitor oxidative folding mechanism a single Fim assisted periplasmic FimC oxidoreductase DsbA. We demonstrate bear high...

10.1038/s41467-018-05107-6 article EN cc-by Nature Communications 2018-07-10

We used single molecule force spectroscopy to characterize the mechanical stability of enhanced yellow fluorescent protein (EYFP) (a mutant form green (GFP)) and two its circularly permutated variants. In all three constructs, we found main unfolding peaks; first corresponds a transition state placed close termini second halfway through molecule. attribute shear rupture beta1- beta6-strands, which verified by introducing point mutation in this region. Although both peaks were observed EYFP...

10.1074/jbc.m609890200 article EN cc-by Journal of Biological Chemistry 2006-11-03

Abstract A major drive in protein folding has been to develop experimental technologies resolve the myriads of microscopic pathways and complex mechanisms that purportedly underlie simple two-state behaviour. This is key for cross-validating predictions from theory modern computer simulations. Detecting such complexity experimentally remained elusive even using methods with improved time, structural or single-molecule resolution. Here, we investigate mechanical unfolding cold shock B (Csp),...

10.1038/ncomms11777 article EN cc-by Nature Communications 2016-06-01

Previously, we identified the protein BBL as a downhill folder. This conclusion was based on statistical mechanical analysis of equilibrium experiments performed in two variants BBL, one with fluorescent label at N-terminus, and another labeled both ends. A recent report has claimed that our results are an artifact label-induced aggregation no labels longer N-terminal tail folds two-state fashion. Here, show singly doubly do not aggregate, unfold reversibly, have same thermodynamic...

10.1021/bi050118y article EN Biochemistry 2005-04-27

Protein folding barriers, which range from zero to the tens of RT that result in classical two-state kinetics, are primarily determined by protein size and structural topology [Plaxco KW, Simons KT, Baker D (1998) J Mol Biol 277:985–994]. Here, we investigate thermodynamic barriers two relatively large proteins same topology: bovine α-lactalbumin (BLA) hen-egg-white lysozyme (HEWL). From analysis differential scanning calorimetry experiments with variable-barrier model [Muñoz V, Sanchez-Ruiz...

10.1073/pnas.0709881105 article EN Proceedings of the National Academy of Sciences 2008-06-13

Inspired by the properties of natural chitin, present work provides first solid foundation for growing conformal ultrathin antibacterial films organic chitin through a solvent-free molecular layer deposition (MLD) process. This establishes initial groundwork biomimetic hybrid cuticles combining sugar-type molecules with vapor-phase metal-organic precursors, which we term metallochitins or, more generally, metallosaccharides. The MLD process, featuring mild temperatures and conditions,...

10.1021/acsami.4c19728 article EN ACS Applied Materials & Interfaces 2025-01-31
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