David
Rodríguez Larrea
Universidad de Granada
Granada, EspañaPublicaciones en colaboración con investigadores/as de Universidad de Granada (16)
2012
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The Peripheral Binding of 14-3-3γ to Membranes Involves Isoform-Specific Histidine Residues
PLoS ONE, Vol. 7, Núm. 11
2010
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Modulation of buried ionizable groups in proteins with engineered surface charge
Journal of the American Chemical Society, Vol. 132, Núm. 4, pp. 1218-1219
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Protein-protein interactions at an enzyme-substrate interface: Characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase
Proteins: Structure, Function and Bioinformatics, Vol. 78, Núm. 1, pp. 36-51
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Proteolytic scanning calorimetry: A novel methodology that probes the fundamental features of protein kinetic stability
Biophysical Journal, Vol. 98, Núm. 6
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Role of conservative mutations in protein multi-property adaptation
Biochemical Journal, Vol. 429, Núm. 2, pp. 243-249
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Using multi-objective computational design to extend protein promiscuity
Biophysical Chemistry, Vol. 147, Núm. 1-2, pp. 13-19
2009
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Between-Species Variation in the Kinetic Stability of TIM Proteins Linked to Solvation-Barrier Free Energies
Journal of Molecular Biology, Vol. 385, Núm. 3, pp. 924-937
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Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy
Nature Structural and Molecular Biology, Vol. 16, Núm. 8, pp. 890-896
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Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes
Journal of Biological Chemistry, Vol. 284, Núm. 47, pp. 32758-32769
2008
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Beyond Lumry-Eyring: An unexpected pattern of operational reversibility/irreversibility in protein denaturation
Proteins: Structure, Function and Genetics, Vol. 70, Núm. 1, pp. 19-24
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Engineering proteins with tunable thermodynamic and kinetic stabilities
Proteins: Structure, Function and Genetics, Vol. 71, Núm. 1, pp. 165-174
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Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis
Journal of Biological Chemistry, Vol. 283, Núm. 40, pp. 27121-27129
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Structural basis of human triosephosphate isomerase deficiency: Mutation E104D is related to alterations of a conserved water network at the dimer interface
Journal of Biological Chemistry, Vol. 283, Núm. 34, pp. 23254-23263
2006
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Energetic and structural consequences of desolvation/solvation barriers to protein folding/unfolding assessed from experimental unfolding rates
Biophysical Journal, Vol. 91, Núm. 5
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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
Journal of Molecular Biology, Vol. 362, Núm. 5, pp. 966-978
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Role of Solvation Barriers in Protein Kinetic Stability
Journal of Molecular Biology, Vol. 360, Núm. 3, pp. 715-724