Published in Biochemistry on March 29, 1983
Imaging the migration pathways for O2, CO, NO, and Xe inside myoglobin. Biophys J (2006) 1.80
Molecular dioxygen enters the active site of 12/15-lipoxygenase via dynamic oxygen access channels. Proc Natl Acad Sci U S A (2007) 1.32
Multiple pathways guide oxygen diffusion into flavoenzyme active sites. Proc Natl Acad Sci U S A (2009) 1.25
Protein compressibility, dynamics, and pressure. Biophys J (2000) 1.16
On the prevalence of room-temperature protein phosphorescence. Science (1987) 1.13
A single-amino-acid lid renders a gas-tight compartment within a membrane-bound transporter. Proc Natl Acad Sci U S A (2004) 1.01
Kinetics of cardiac thin-filament activation probed by fluorescence polarization of rhodamine-labeled troponin C in skinned guinea pig trabeculae. Biophys J (2005) 0.94
Quenching of alkaline phosphatase phosphorescence by O2 and NO. Evidence for inflexible regions of protein structure. Biophys J (1987) 0.93
Long-range electron exchange measured in proteins by quenching of tryptophan phosphorescence. Proc Natl Acad Sci U S A (1990) 0.91
Time-resolved room temperature protein phosphorescence: nonexponential decay from single emitting tryptophans. Biophys J (1994) 0.89
Polarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges. Biophys J (2002) 0.89
Excited states of tryptophan in cod parvalbumin. Identification of a short-lived emitting triplet state at room temperature. Biophys J (1993) 0.88
Probing protein conformation with a minimal photochemical reagent. Protein Sci (2002) 0.87
Mapping oxygen accessibility to ribonuclease a using high-resolution NMR relaxation spectroscopy. Biophys J (2004) 0.87
Fluorescent protein barrel fluctuations and oxygen diffusion pathways in mCherry. J Chem Phys (2011) 0.86
Oxidized amino acid residues in the vicinity of Q(A) and Pheo(D1) of the photosystem II reaction center: putative generation sites of reducing-side reactive oxygen species. PLoS One (2013) 0.83
Detecting O2 binding sites in protein cavities. Sci Rep (2016) 0.78
Gated quenching of intrinsic fluorescence and phosphorescence of globular proteins. An extended model. Biophys J (1986) 0.77
Oxygen diffusion pathways in a cofactor-independent dioxygenase. Chem Sci (2015) 0.75
Primary structure effects on peptide group hydrogen exchange. Proteins (1993) 10.79
Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q Rev Biophys (1983) 9.14
Protein folding intermediates: native-state hydrogen exchange. Science (1995) 5.91
Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature (1988) 4.57
Primary structure effects on peptide group hydrogen exchange. Biochemistry (1972) 4.08
An optical method for measurement of dioxygen concentration based upon quenching of phosphorescence. J Biol Chem (1987) 3.46
Hydrogen exchange. Annu Rev Biochem (1972) 3.31
Isotope effects in peptide group hydrogen exchange. Proteins (1993) 3.21
Imaging of phosphorescence: a novel method for measuring oxygen distribution in perfused tissue. Science (1988) 2.92
The barriers in protein folding. Nat Struct Biol (1994) 2.79
Stable submolecular folding units in a non-compact form of cytochrome c. J Mol Biol (1991) 2.67
Protein stability parameters measured by hydrogen exchange. Proteins (1994) 2.55
The oxygen dependence of mitochondrial oxidative phosphorylation measured by a new optical method for measuring oxygen concentration. J Biol Chem (1988) 2.25
Protein hydrogen exchange studied by the fragment separation method. Anal Biochem (1985) 2.12
Nature of the open state in long polynucleotide double helices: possibility of soliton excitations. Proc Natl Acad Sci U S A (1980) 2.10
Water magnetic relaxation dispersion in biological systems: the contribution of proton exchange and implications for the noninvasive detection of cartilage degradation. Proc Natl Acad Sci U S A (2001) 2.07
Measurement of structural and free energy changes in hemoglobin by hydrogen exchange methods. Ann N Y Acad Sci (1975) 2.04
Measurement and calibration of peptide group hydrogen-deuterium exchange by ultraviolet spectrophotometry. Anal Biochem (1979) 2.01
Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins (1996) 1.95
Pyrene. A probe of lateral diffusion in the hydrophobic region of membranes. Biochemistry (1974) 1.94
Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR. Biochemistry (1990) 1.94
Determinants of protein hydrogen exchange studied in equine cytochrome c. Protein Sci (1998) 1.92
Base-pair opening and closing reactions in the double helix. A stopped-flow hydrogen exchange study in poly(rA).poly(rU). J Mol Biol (1979) 1.91
Open states in native polynucleotides. I. Hydrogen-exchange study of adenine-containing double helices. J Mol Biol (1975) 1.88
An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR. Science (1990) 1.86
Open states in native polynucleotides. II. Hydrogen-exchange study of cytosine-containing double helices. J Mol Biol (1975) 1.84
Chaperonin function: folding by forced unfolding. Science (1999) 1.83
Climate change and the integrity of science. Science (2010) 1.80
The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. Nat Struct Biol (1998) 1.78
Fluorescence energy transfer between Ca2+ transport ATPase molecules in artificial membranes. Biochemistry (1977) 1.78
Biochemistry without oxygen. Anal Biochem (1987) 1.77
Temperature dependence of 1,6-diphenyl-1,3,5-hexatriene fluorescence in phophoslipid artificial membranes. Biochemistry (1976) 1.76
Oxygen diffusion in biological and artificial membranes determined by the fluorochrome pyrene. J Gen Physiol (1975) 1.73
Future directions in folding: the multi-state nature of protein structure. Proteins (1996) 1.70
Two-dimensional 1H NMR studies of cytochrome c: hydrogen exchange in the N-terminal helix. Biochemistry (1986) 1.69
Thermodynamic parameters from hydrogen exchange measurements. Methods Enzymol (1995) 1.63
Experimental study of the protein folding landscape: unfolding reactions in cytochrome c. J Mol Biol (1999) 1.59
The role of helix formation in the folding of a fully alpha-helical coiled coil. Proteins (1996) 1.58
Metallocytochromes c: characterization of electronic absorption and emission spectra of Sn4+ and Zn2+ cytochromes c. Eur J Biochem (1976) 1.53
Hydrogen-tritium exchange. Methods Enzymol (1972) 1.48
An amino acid code for protein folding. Proc Natl Acad Sci U S A (2001) 1.45
Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C. Proc Natl Acad Sci U S A (1997) 1.42
Evidence for an unfolding and refolding pathway in cytochrome c. Nat Struct Biol (1998) 1.38
Physical properties of biological membranes determined by the fluorescence of the calcium ionophore A23187. Arch Biochem Biophys (1974) 1.36
Ultrafast signals in protein folding and the polypeptide contracted state. Proc Natl Acad Sci U S A (1997) 1.35
Cytochrome c interaction with membranes. Absorption and emission spectra and binding characteristics of iron-free cytochrome c. Eur J Biochem (1975) 1.34
Quenching of room temperature protein phosphorescence by added small molecules. Biochemistry (1988) 1.27
Hydrogen exchange study of some polynucleotides and transfer RNA. J Mol Biol (1972) 1.27
Proton resonance assignments of horse ferrocytochrome c. Biochemistry (1989) 1.25
Individual breathing reactions measured in hemoglobin by hydrogen exchange methods. Biophys J (1980) 1.22
Hydrogen--tritium exchange. Methods Enzymol (1978) 1.21
Conformational relaxation of a low-temperature protein as probed by photochemical hole burning. Horseradish peroxidase. Biophys J (1991) 1.20
Site-selected fluorescence spectra of porphyrin derivatives of heme proteins. Biochemistry (1985) 1.19
Hydrogen bond strength and beta-sheet propensities: the role of a side chain blocking effect. Proteins (1994) 1.18
Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence. Biochemistry (1983) 1.18
More than two pyrrole tautomers of mesoporphyrin stabilized by a protein. High resolution optical spectroscopic study. Biophys J (1992) 1.17
Two-state vs. multistate protein unfolding studied by optical melting and hydrogen exchange. Protein Sci (2000) 1.17
Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR. Biochemistry (1992) 1.16
Proton resonance assignments of horse ferricytochrome c. Biochemistry (1989) 1.15
Rapid microdialysis and hydrogen exchange. Anal Biochem (1965) 1.13
Identification of an allosterically sensitive unfolding unit in hemoglobin. J Mol Biol (1983) 1.13
On the prevalence of room-temperature protein phosphorescence. Science (1987) 1.13
Redox-dependent structure change and hyperfine nuclear magnetic resonance shifts in cytochrome c. Biochemistry (1990) 1.11
Reactions of excited triplet states of metal substituted myoglobin with dioxygen and quinone. Biophys J (1990) 1.08
Measuring the conformational stability of a protein by hydrogen exchange. Methods Mol Biol (2001) 1.08
Oxygen diffusion in phospholipid artificial membranes studied by Fourier transform nuclear magnetic resonance. Arch Biochem Biophys (1979) 1.05
Interaction of general anesthetics with phospholipid vesicles and biological membranes. Biochim Biophys Acta (1977) 1.04
Two-dimensional 1H NMR studies of cytochrome c: assignment of the N-terminal helix. Biochemistry (1986) 1.03
Protein-induced changes in nonplanarity of the porphyrin in nickel cytochrome c probed by resonance Raman spectroscopy. Biochemistry (1998) 1.03
Metal-free and metal-substituted cytochromes c. Use in characterization of the cytochrome c binding site. Eur J Biochem (1977) 1.02
Infrared spectroscopy of the cyanide complex of iron (II) myoglobin and comparison with complexes of microperoxidase and hemoglobin. Biochemistry (1996) 1.00
Individual breathing reactions measured by functional labeling and hydrogen exchange methods. Methods Enzymol (1986) 1.00
Tryptophan phosphorescence at room temperature as a tool to study protein structure and dynamics. Photochem Photobiol (1989) 0.99
Softening of the packing density of horseradish peroxidase by a H-donor bound near the heme pocket. Biophys J (1992) 0.98
Resolved fluorescence emission spectra of iron-free cytochrome c. Photochem Photobiol (1982) 0.98
Protein fluorescence quenching by small molecules: protein penetration versus solvent exposure. Proteins (1986) 0.98
Sickle hemoglobin gelation. Reaction order and critical nucleus size. Biophys J (1978) 0.96
The slowest allosterically responsive hydrogens in hemoglobin. Completion of the hydrogen exchange survey. J Biol Chem (1980) 0.96
Differences in the binding of aromatic substrates to horseradish peroxidase revealed by fluorescence line narrowing. Biochemistry (1989) 0.96
Protein complexes studied by NMR spectroscopy. Curr Opin Biotechnol (1996) 0.95
Structure of zinc-substituted cytochrome c: nuclear magnetic resonance and optical spectroscopic studies. Biochemistry (1995) 0.95
Allosteric energy at the hemoglobin beta chain C terminus studied by hydrogen exchange. J Mol Biol (1988) 0.95
Hydrogen exchange. Nat Struct Biol (2001) 0.95
Effects of growth temperature and supplementation with exogenous fatty acids on some physical properties of Clostridium butyricum phospholipids. Biochim Biophys Acta (1977) 0.94
Allosteric sensitivity in hemoglobin at the alpha-subunit N-terminus studied by hydrogen exchange. Biochemistry (1986) 0.94
Hydrogen exchnge studies of respiratory proteins. II. Detection of discrete, ligand-induced changes in hemoglobin. J Biol Chem (1972) 0.94
Dynamics of parvalbumin studied by fluorescence emission and triplet absorption spectroscopy of tryptophan. Biochemistry (1995) 0.94
Native collagen has a two-bonded structure. J Mol Biol (1974) 0.93
Measurement of the free and the H-bonded amides of myoglobin. J Mol Biol (1969) 0.93
Hydrogen-exchange measurements on Escherichia coli transfer ribonucleic acid before, after, and during its aminoacylation. Biochemistry (1969) 0.93