Published in Biophys J on December 22, 2006
Heterogeneity in desiccated solutions: implications for biostabilization. Biophys J (2007) 0.91
Structural characterization of IgG1 mAb aggregates and particles generated under various stress conditions. J Pharm Sci (2014) 0.88
In situ spectroscopic quantification of protein-ice interactions. J Phys Chem B (2013) 0.85
Conversion of stable RNA hairpin to a metastable dimer in frozen solution. RNA (2007) 0.84
Freezing-induced perturbation of tertiary structure of a monoclonal antibody. J Pharm Sci (2014) 0.81
Microheterogeneity in frozen protein solutions. Int J Pharm (2015) 0.76
Cavity-creating mutations in Pseudomonas aeruginosa azurin: effects on protein dynamics and stability. Biophys J (2008) 0.76
Protein freeze concentration and micro-segregation analysed in a temperature-controlled freeze container. Biotechnol Rep (Amst) (2015) 0.75
Protein brownian rotation at the glass transition temperature of a freeze-concentrated buffer probed by superparamagnetic nanoparticles. Biophys J (2013) 0.75
Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol (1986) 12.22
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci (1995) 9.23
Psychrophilic enzymes: hot topics in cold adaptation. Nat Rev Microbiol (2003) 3.18
The preparation of guanidine hydrochloride. Methods Enzymol (1972) 3.13
Psychrophilic microorganisms: challenges for life. EMBO Rep (2006) 2.57
Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip. J Mol Biol (1991) 2.19
Fluorescence techniques for studying protein structure. Methods Biochem Anal (1991) 2.12
Linear extrapolation method of analyzing solvent denaturation curves. Proteins (2000) 1.72
Proteins in frozen solutions: evidence of ice-induced partial unfolding. Biophys J (1996) 1.28
Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli. FEBS Lett (1989) 1.18
Surface-induced denaturation of proteins during freezing and its inhibition by surfactants. J Pharm Sci (1996) 1.17
Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. II. Structural studies using infrared spectroscopy. Arch Biochem Biophys (1993) 1.14
Crystal structure of Pseudomonas aeruginosa apo-azurin at 1.85 A resolution. FEBS Lett (1992) 1.13
The effect of pressure and guanidine hydrochloride on azurins mutated in the hydrophobic core. Eur J Biochem (1999) 1.09
Studies of thermally induced denaturation of azurin and azurin derivatives by differential scanning calorimetry: evidence for copper selectivity. Biochemistry (1986) 1.03
Separation of freezing- and drying-induced denaturation of lyophilized proteins using stress-specific stabilization. I. Enzyme activity and calorimetric studies. Arch Biochem Biophys (1993) 1.01
Approaching the speed limit for Greek Key beta-barrel formation: transition-state movement tunes folding rate of zinc-substituted azurin. Biochim Biophys Acta (2003) 0.92
Perturbation of protein tertiary structure in frozen solutions revealed by 1-anilino-8-naphthalene sulfonate fluorescence. Biophys J (2003) 0.91
ANS fluorescence detects widespread perturbations of protein tertiary structure in ice. Biophys J (2006) 0.89
Effects of metal ligation and oxygen on the reversibility of the thermal denaturation of Pseudomonas aeruginosa azurin. Biochemistry (2002) 0.88
Apo-azurin folds via an intermediate that resembles the molten-globule. Protein Sci (2004) 0.84
Interactions between PEG and type I soluble tumor necrosis factor receptor: modulation by pH and by PEGylation at the N terminus. Protein Sci (2002) 0.87
The triplet-state lifetime of indole derivatives in aqueous solution. Photochem Photobiol (2004) 0.85
The tryptophan phosphorescence of porcine and mutant bovine odorant-binding proteins: a probe for the local protein structure and dynamics. J Proteome Res (2008) 0.82
Fluorescence quenching of buried Trp residues by acrylamide does not require penetration of the protein fold. J Phys Chem B (2010) 0.81
Singular efficacy of trimethylamine N-oxide to counter protein destabilization in ice. Biochemistry (2008) 0.79
Tryptophan phosphorescence studies of the D-galactose/D-glucose-binding protein from Escherichia coli provide a molecular portrait with structural and dynamics features of the protein. J Proteome Res (2007) 0.78
Acrylonitrile quenching of trp phosphorescence in proteins: a probe of the internal flexibility of the globular fold. Biophys J (2010) 0.78
Effects of sugars and polyols on the stability of azurin in ice. J Phys Chem B (2008) 0.78
Structure and dynamics of cold-adapted enzymes as investigated by phosphorescence spectroscopy and molecular dynamics studies. 2. The case of an esterase from Pseudoalteromonas haloplanktis. J Phys Chem B (2009) 0.77
Specific anions effects of on the stability of azurin in ice. J Phys Chem B (2008) 0.77
Acrylamide quenching of Trp phosphorescence in liver alcohol dehydrogenase: evidence of gated quencher penetration. Biochemistry (2009) 0.77
Protein phosphorescence quenching: distinction between quencher penetration and external quenching mechanisms. J Phys Chem B (2010) 0.77
Amplitude spectrum of structural fluctuations in proteins from the internal diffusion of solutes of increasing molecular size: a Trp phosphorescence quenching study. Biochemistry (2011) 0.77
Characterization of f-actin tryptophan phosphorescence in the presence and absence of tryptophan-free myosin motor domain. Biophys J (2004) 0.76
Mutations in transhydrogenase change the fluorescence emission state of TRP72 from 1La to 1Lb. Biophys J (2008) 0.75
Influence of denaturants on native-state structural fluctuations in azurin probed by molecular size-dependent quenching of Trp phosphorescence. J Phys Chem B (2011) 0.75