Published in Proteins on August 01, 1997
The helical alanine controversy: an (Ala)6 insertion dramatically increases helicity. J Am Chem Soc (2004) 1.11
CD spectroscopy of peptides and proteins bound to large unilamellar vesicles. J Membr Biol (2010) 1.04
Statistical prediction and molecular dynamics simulation. Biophys J (2008) 0.78
Blue dextran-sepharose: an affinity column for the dinucleotide fold in proteins. Proc Natl Acad Sci U S A (1975) 4.40
Measurement of protein concentration with interferences optics. Anal Biochem (1969) 2.31
Binding of Cibacron blue F3GA to proteins containing the dinucleotide fold. Proc Natl Acad Sci U S A (1976) 2.16
Residue helix parameters obtained from dichroic analysis of peptides of defined sequence. Biochemistry (1993) 1.61
Effect of central-residue replacements on the helical stability of a monomeric peptide. Biochemistry (1990) 1.47
Manipulation of the observed kinetic phases in the refolding of denatured ferricytochromes c. J Biol Chem (1983) 1.36
Haem exposure as the determinate of oxidation-reduction potential of haem proteins. Nature (1978) 1.33
Participation of the protein ligands in the folding of cytochrome c. Biochemistry (1972) 1.32
The role of PII conformations in the calculation of peptide fractional helix content. Protein Sci (1997) 1.23
Carboxymethylation of horse heart ferricytochrome c and cyanferricytochrome c. Biochemistry (1968) 1.22
Effect of amino acid ion pairs on peptide helicity. Biochemistry (1991) 1.17
Positional independence and additivity of amino acid replacements on helix stability in monomeric peptides. Biochemistry (1990) 1.13
Purification of a cyclic nucleotide phosphodiesterase from bovine brain using blue dextran-Sepharose chromatography. J Biol Chem (1979) 1.12
A model peptide with enhanced helicity. Biochemistry (1991) 1.11
Purification and subunit structure of glutathione reductase from bakers' yeast. J Biol Chem (1968) 1.08
Relationship of protein thermostability to accessible surface area. Nature (1978) 1.08
The conformation of horse heart apocytochrome c. J Biol Chem (1972) 1.06
Equilibrium and kinetic measurements of the conformational transition of reduced thioredoxin. Biochemistry (1987) 1.05
The effect of proteolysis on the calmodulin activation of cyclic nucleotide phosphodiesterase. J Biol Chem (1981) 1.05
A thermostable enolase from the extreme thermophile Thermus aquaticus YT-1. Biochemistry (1973) 1.03
Nuclear magnetic resonance study of the rate of electron transfer between cytochrome c and iron hexacyanides. J Mol Biol (1973) 1.00
Stabilization of the globular structure of ferricytochrome c by chloride in acidic solvents. Biochemistry (1975) 0.99
Prediction of neutral salt elution profiles for affinity chromatography. Proc Natl Acad Sci U S A (1981) 0.98
Conformational transitions of thioredoxin in guanidine hydrochloride. Biochemistry (1984) 0.95
Enolase from the thermophile Thermus X-1. Biochemistry (1973) 0.95
Nuclear magnetic resonance study of exchangeable protons in ferrocytochrome c. J Mol Biol (1973) 0.95
Proposed structure for brain adenylate cyclase purified using blue dextran-Sepharose chromatography. Nature (1976) 0.94
The role of cations in yeast phosphofructokinase catalysis. J Biol Chem (1970) 0.93
Reactivity of individual tyrosyl residues of horse heart ferricytochrome c toward iodination. Biochemistry (1970) 0.93
Refolding a disulfide dimer of cytochrome c. Biochemistry (1985) 0.92
The existence of heme-protein coordinate-covalent bonds in denaturing solvents. Biopolymers (1971) 0.91
Alkaline isomerization of ferricytochrome C from Euglena gracilis. Biochem Biophys Res Commun (1974) 0.88
Purification and properties of phosphofructokinase from yeast. J Biol Chem (1968) 0.87
Incorporation of pairwise interactions into the Lifson-Roig model for helix prediction. Protein Sci (1995) 0.87
Effects of guanidine hydrochloride on the refolding kinetics of denatured thioredoxin. Biochemistry (1986) 0.87
Gel filtration. Methods Enzymol (1990) 0.87
The reversible unfolding of horse heart ferricytochrome c. Biochemistry (1968) 0.86
Limited proteolysis of yeast phosphofructokinase. Sequence locations of cleavage sites created by the actions of different proteinases. Eur J Biochem (1993) 0.86
Analysis of peptides for helical prediction. Biochemistry (1989) 0.85
Alkaline isomerization of ferricytochrome c: identification of the lysine ligand. Proc Natl Acad Sci U S A (1974) 0.84
A rapid purification of T4 polynucleotide kinase using Blue Dextran-Sepharose chromatography. Biochim Biophys Acta (1978) 0.83
Analysis of N-terminal capping using carbonyl-carbon chemical shift measurements. Proteins (1998) 0.83
Activation of Thermus phosphofructokinase by monovalent cations. Biochim Biophys Acta (1979) 0.83
A monoisozymic nucleoside diphosphate kinase capable of complete phosphorylation. J Biol Chem (1981) 0.82
Spectral and electrochemical studies of cytochrome c peptide complexes. J Biol Chem (1978) 0.82
The alkaline isomerization of lysine-modified ferricytochrome c. Biochim Biophys Acta (1975) 0.82
Proline peptide isomerization and the reactivation of denatured enzymes. J Mol Biol (1979) 0.81
Spectral studies of horse heart porphyrin cytochrome c. J Biol Chem (1984) 0.80
Affinity chromatography in nonionic detergent solutions. Proc Natl Acad Sci U S A (1980) 0.80
Conformational transitions of frog heart ferricytochrome c. Biochemistry (1982) 0.80
Predicted structure for aldolase. J Mol Biol (1976) 0.80
Location of the heme moiety of cytochrome c by solvent perturbation. J Biol Chem (1967) 0.79
Modulation of the helical stability of a model peptide by ionic residues. Biochemistry (1993) 0.79
The structure of hemopeptide 1-65 from cytochrome c. Arch Biochem Biophys (1972) 0.79
Characterization of guanidinated cytochrome c by 13C nuclear magnetic resonance spectroscopy. Biochemistry (1977) 0.78
Interaction of Cibacron Blue F3GA with Escherichia coli DNA polymerase I and with T4 DNA polymerase. Biochim Biophys Acta (1979) 0.78
Phosphofructokinase of yeast. Methods Enzymol (1975) 0.78
Equilibrium and kinetic measurements of the conformational transition of thioredoxin in urea. Biochemistry (1986) 0.78
Kinetic analysis of the hydrodynamic transition accompanying protein folding using size exclusion chromatography. 2. Comparison of spectral and chromatographic kinetic analyses. Biopolymers (1993) 0.78
Chromatography on immobilized reactive dyes. Methods Enzymol (1990) 0.77
Refolding of denatured ribonuclease observed by size exclusion chromatography. Biochemistry (1989) 0.77
Carboxymethylation of the histidyl residues of horse heart cytochrome c. Biochem Biophys Res Commun (1966) 0.77
Complexation of iron hexacyanides by cytochrome c. Evidence for electron exchange at the exposed heme edge. J Biol Chem (1975) 0.77
Structural location of the tyrosyl and tryptophanyl residues of tuna heart cytochrome c. Biochemistry (1970) 0.77
Conformational transitions of a cytochrome c having a single thioether bridge. J Biol Chem (1983) 0.76
Quantitative analysis of protein: immobilized dye interaction. J Biol Chem (1984) 0.76
Advantages of preelectrophoretic conjugation of polypeptides with fluorescent dyes. Anal Biochem (1983) 0.76
A globular high spin form of ferricytochrome c. J Biol Chem (1983) 0.76
The molecular weight of the polypeptide chains of yeast phosphofructokinase. Biochem Biophys Res Commun (1971) 0.76
A quantitative procedure for recovery of nucleoside phosphate ligands and preparation of apoprotein from holoproteins using blue dextran--Sepharose chromatography. Anal Biochem (1976) 0.76
An examination of the involvement of proline peptide isomerization in protein folding. J Mol Biol (1978) 0.75
Calibration mixture for estimation of peptide molecular weight by exclusion chromatography. Anal Biochem (1979) 0.75
Accessibility and multivalency of immobilized Cibacron blue F3GA. J Biol Chem (1987) 0.75
The effect of methylation on cytochrome c fragment complementation. J Biol Chem (1981) 0.75
The conformational transition of horse heart porphyrin c. J Biol Chem (1982) 0.75
Kinetic analysis of the hydrodynamic transition accompanying protein folding using size exclusion chromatography. 1. Denaturant dependent baseline changes. Biopolymers (1993) 0.75
Protein dye affinity chromatography using immobilized tetraiodofluorescein. J Biol Chem (1981) 0.75
Preparation and analysis of reactive blue 2 bonded to silica via variable spacer groups. J Chromatogr (1984) 0.75
A kinetic study of the folding of staphylococcal nuclease using size-exclusion chromatography. Biochemistry (1992) 0.75
Strategies for increasing the stability of enzymes. Ann N Y Acad Sci (1984) 0.75
Zonal chromatographic analysis of the interaction of alcohol dehydrogenase with blue-sepharose. J Chromatogr (1986) 0.75
A reexamination of the conformational transitions of T4 thioredoxin. Biopolymers (1993) 0.75
A Thermostable phosphofructokinase from the extreme thermophile Thermus X-1. Arch Biochem Biophys (1975) 0.75
Refolding of denatured thioredoxin observed by size-exclusion chromatography. Biochemistry (1987) 0.75
Midpoint potentials of cytochromes in vesicles of anaerobically-grown Paracoccus denitrificans determined by the indirect coulometric titration method. Biochim Biophys Acta (1981) 0.75
Analysis of the thermostability of enolases. Experientia Suppl (1976) 0.75
The structural environment of the tryptophanyl residue of horse heart ferricytochrome c. J Biol Chem (1967) 0.75
A structure for calmodulin-activated cyclic nucleotide phosphodiesterase deduced from proteolysis studies. Adv Cyclic Nucleotide Protein Phosphorylation Res (1984) 0.75
Deletion of the terminal sequences from cytochromes c. J Biol Chem (1985) 0.75