Lista de obras - David Rodríguez-Larrea - Dominio Público Uruguay

Between-species variation in the kinetic stability of TIM proteins linked to solvation-barrier free energies.

artículo científico publicado en 2008

Beyond Lumry-Eyring: An unexpected pattern of operational reversibility/irreversibility in protein denaturation

artículo científico publicado en 2008

Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy.

artículo científico publicado en 2009

Energetic and structural consequences of desolvation/solvation barriers to protein folding/unfolding assessed from experimental unfolding rates

artículo científico publicado en 2006

Engineering proteins with tunable thermodynamic and kinetic stabilities.

artículo científico publicado en 2008

Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis

artículo científico publicado en 2008

Free-energy landscapes of membrane co-translocational protein unfolding

scientific article published on 03 April 2020

Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

artículo científico publicado en 2013

Label-Free, Multiplexed, Single-Molecule Analysis of Protein-DNA Complexes with Nanopores

artículo científico publicado en 2017

Modulation of buried ionizable groups in proteins with engineered surface charge.

artículo científico publicado en 2010

Multistep protein unfolding during nanopore translocation

artículo científico publicado en 2013

Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments.

artículo científico publicado en 2006

Protein co-translocational unfolding depends on the direction of pulling

artículo científico publicado en 2014

Protein-protein interactions at an enzyme-substrate interface: characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase.

artículo científico publicado en 2010

Proteolytic scanning calorimetry: a novel methodology that probes the fundamental features of protein kinetic stability

artículo científico publicado en 2010

Role of conservative mutations in protein multi-property adaptation

artículo científico publicado en 2010

Role of solvation barriers in protein kinetic stability.

artículo científico publicado en 2006

Single-molecule site-specific detection of protein phosphorylation with a nanopore

artículo científico publicado en 2014

Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface

artículo científico publicado en 2008

The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues

artículo científico publicado en 2012

Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes

artículo científico publicado en 2009

Transmembrane protein rotaxanes reveal kinetic traps in the refolding of translocated substrates

scientific article published on 03 April 2020

Using multi-objective computational design to extend protein promiscuity.

artículo científico publicado en 2010

Lista de obras de David Rodríguez-Larrea

Between-species variation in the kinetic stability of TIM proteins linked to solvation-barrier free energies.

Beyond Lumry-Eyring: An unexpected pattern of operational reversibility/irreversibility in protein denaturation

Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy.

Energetic and structural consequences of desolvation/solvation barriers to protein folding/unfolding assessed from experimental unfolding rates

Engineering proteins with tunable thermodynamic and kinetic stabilities.

Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis

Free-energy landscapes of membrane co-translocational protein unfolding

Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

Label-Free, Multiplexed, Single-Molecule Analysis of Protein-DNA Complexes with Nanopores

Modulation of buried ionizable groups in proteins with engineered surface charge.

Multistep protein unfolding during nanopore translocation

Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments.

Protein co-translocational unfolding depends on the direction of pulling

Protein-protein interactions at an enzyme-substrate interface: characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase.

Proteolytic scanning calorimetry: a novel methodology that probes the fundamental features of protein kinetic stability

Role of conservative mutations in protein multi-property adaptation

Role of solvation barriers in protein kinetic stability.

Single-molecule site-specific detection of protein phosphorylation with a nanopore

Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface

The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues

Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes

Transmembrane protein rotaxanes reveal kinetic traps in the refolding of translocated substrates

Using multi-objective computational design to extend protein promiscuity.