Published in Ann N Y Acad Sci on January 01, 1973
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Ozone model for bonding of an O2 to heme in oxyhemoglobin. Proc Natl Acad Sci U S A (1975) 1.76
Structure of hemoglobin S fibers: optical determination of the molecular orientation in sickled erythrocytes. Proc Natl Acad Sci U S A (1973) 1.72
Kinetics of carboxymyoglobin and oxymyoglobin studied by picosecond spectroscopy. Biophys J (1979) 1.39
Photoselection in polarized photolysis experiments on heme proteins. Biophys J (1993) 1.23
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Measuring the rate of intramolecular contact formation in polypeptides. Proc Natl Acad Sci U S A (2000) 3.64
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Conformational relaxation and ligand binding in myoglobin. Biochemistry (1994) 2.71
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Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation. Proc Natl Acad Sci U S A (1978) 2.15
Electronic spectrum of single crystals of ferricytochrome-c. J Chem Phys (1967) 2.00
Thermodynamics of gelation of sickle cell deoxyhemoglobin. J Mol Biol (1977) 1.97
Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin. Proc Natl Acad Sci U S A (1985) 1.94
Structure of carboxymyoglobin in crystals and in solution. Proc Natl Acad Sci U S A (1979) 1.79
Protein reaction kinetics in a room-temperature glass. Science (1995) 1.77
Geminate recombination of carbon monoxide to myoglobin. J Mol Biol (1983) 1.75
Structure of hemoglobin S fibers: optical determination of the molecular orientation in sickled erythrocytes. Proc Natl Acad Sci U S A (1973) 1.72
Calorimetric and optical characterization of sickle cell hemoglobin gelation. J Mol Biol (1975) 1.67
Delay time of hemoglobin S polymerization prevents most cells from sickling in vivo. Science (1987) 1.61
Gelation of sickle cell hemoglobin in mixtures with normal adult and fetal hemoglobins. J Mol Biol (1979) 1.58
Requirement for therapeutic inhibition of sickle haemoglobin gelation. Nature (1978) 1.58
Oxygen binding by sickle cell hemoglobin polymers. J Mol Biol (1982) 1.58
Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect. Nature (1991) 1.56
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A multiparameter analysis of sickle erythrocytes in patients undergoing hydroxyurea therapy. Blood (1996) 1.39
The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin. Proc Natl Acad Sci U S A (1988) 1.36
Speed of intersubunit communication in proteins. Biochemistry (1992) 1.35
Molecular and cellular pathogenesis of hemoglobin SC disease. Proc Natl Acad Sci U S A (1982) 1.32
Two-state expansion and collapse of a polypeptide. J Mol Biol (2000) 1.31
Biochemical studies of skeletal muscle mitochondria. I. Microanalysis of cytochrome content, oxidative and phosphorylative activities of mammalian skeletal muscle mitochondria. Arch Biochem Biophys (1968) 1.31
Dynamics of intramolecular contact formation in polypeptides: distance dependence of quenching rates in a room-temperature glass. Phys Rev Lett (2001) 1.28
Hydrolysis of esters by carboxypeptidase A requires a penta-coordinate metal ion. J Biol Chem (1982) 1.27
Catalytic role of the metal ion of carboxypeptidase A in ester hydrolysis. J Biol Chem (1979) 1.27
Editorial: Delay time of gelation: a possible determinant of clinical severity in sickle cell disease. Blood (1976) 1.26
Low-frequency Raman spectra of lysozyme. Biopolymers (1976) 1.24
Photoselection in polarized photolysis experiments on heme proteins. Biophys J (1993) 1.23
Dynamics of the quaternary conformational change in trout hemoglobin. Biochemistry (1991) 1.22
Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication. Biochemistry (1985) 1.22
Optically detected conformational changes in haemoglobin single crystals. Nature (1974) 1.20
Linear dichroism of biological chromophores. Annu Rev Biophys Bioeng (1976) 1.20
Time-resolved optical spectroscopy and structural dynamics following photodissociation of carbonmonoxyhemoglobin. Biophys Chem (1988) 1.20
Oxygen binding by single crystals of hemoglobin. Biochemistry (1993) 1.16
Can a two-state MWC allosteric model explain hemoglobin kinetics? Biochemistry (1997) 1.16
The relationship between coding sequences and function in haemoglobin. Nature (1980) 1.16
Electron microscopy of fibers and discs of hemoglobin S having sixfold symmetry. Proc Natl Acad Sci U S A (1977) 1.16
Protonation of the beta-lactam nitrogen is the trigger event in the catalytic action of class A beta-lactamases. Proc Natl Acad Sci U S A (2000) 1.14
Kinetics of sickle haemoglobin polymerization in single red cells. Nature (1982) 1.12
Reactivity and cryoenzymology of enzymes in the crystalline state. Annu Rev Biophys Bioeng (1977) 1.12
Polarized single-crystal absorption spectrum of 1-methyluracil. J Chem Phys (1970) 1.11
Tetrahedral iron in the active center of plant ferredoxins and beef adrenodoxin. Proc Natl Acad Sci U S A (1971) 1.04
In vivo spin-label murine pharmacodynamics using low-frequency electron paramagnetic resonance imaging. Biophys J (1996) 1.03
Comparison of sickle cell hemoglobin gelation kinetics measured by NMR and optical methods. Biochem Biophys Res Commun (1976) 1.02
Near-infrared absorption and circular dichroism spectra of ferrocytochrome c: d-d transitions. J Chem Phys (1969) 1.01
Mechanism of action of carboxypeptidase A in ester hydrolysis. Proc Natl Acad Sci U S A (1976) 1.01
Overexpression and biosynthetic deuterium enrichment of TEM-1 beta-lactamase for structural characterization by magnetic resonance methods. Protein Expr Purif (2000) 0.98
Simulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin. Proc Natl Acad Sci U S A (1993) 0.98
Thermodynamic aspects of the potassium hexacyanoferrate(3)-(2) system. II. Reduction potential. J Phys Chem (1967) 0.97
Letter: Origin of the anomalous Soret spectra of carboxycytochrome P-450. J Am Chem Soc (1976) 0.97
Near-infrared circular dichroism of an iron-sulfur protein. D leads to d transitions in rubredoxin. J Am Chem Soc (1970) 0.96
Optical triggers of protein folding. Science (1996) 0.95
Optical spectra and electronic structure of flavine mononucleotide in flavodoxin crystals. Biochemistry (1975) 0.94
Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals. Protein Sci (1997) 0.93
Coordination environment of the active-site metal ion of liver alcohol dehydrogenase. Proc Natl Acad Sci U S A (1981) 0.92
Two-state expansion and collapse of a polypeptide. J Mol Biol (2000) 0.92
Picosecond transient absorption study of photodissociated carboxy hemoglobin and myoglobin. Biophys J (1988) 0.92
Oxygen binding by single crystals of hemoglobin: the problem of cooperativity and inequivalence of alpha and beta subunits. Proteins (1996) 0.90
Mg2+ is not catalytically required in the intrinsic and kirromycin-stimulated GTPase action of Thermus thermophilus EF-Tu. J Biol Chem (2001) 0.89
Heme-heme orientation and electron transfer kinetic behavior of multisite oxidation-reduction enzymes. Science (1983) 0.89
Fe-O2 bonding and oxyheme structure in myoglobin. Proc Natl Acad Sci U S A (1978) 0.88
Electron microscope study of the kinetics of the fiber-to-crystal transition of sickle cell hemoglobin. Proc Natl Acad Sci U S A (1980) 0.88
Structural basis and dynamics of the fiber-to-crystal transition of sickle cell hemoglobin. J Mol Biol (1984) 0.88
Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenase. Proc Natl Acad Sci U S A (1983) 0.86
Catalytic conformation of carboxypeptidase A. Structure of a true enzyme reaction intermediate determined by electron nuclear double resonance. J Biol Chem (1994) 0.86
Structure and mechanism of carboxypeptidase A. Adv Inorg Biochem (1984) 0.86
Correlation of polarized absorption spectroscopic and X-ray diffraction studies of crystalline cytosolic aspartate aminotransferase of pig hearts. J Mol Biol (1988) 0.83
Catalytic conformation of carboxypeptidase A. The structure of a true reaction intermediate stabilized at subzero temperatures. J Mol Biol (1983) 0.81
Comments on the physics and chemistry of trehalose as a storage medium for hemoglobin-based blood substitutes: "from Kramers Theory to the Battlefield". Transfus Clin Biol (1995) 0.81
Specificity of interaction of haptoglobin with mammalian hemoglobin. Biochemistry (1972) 0.80
Synthesis of chromophoric, spin label enzyme substrates useful for cryoenzymology. J Biol Chem (1979) 0.80
A crystallographic study of deoxy cobalt (II) mesoporphyrin IX myoglobin. J Biol Chem (1975) 0.80
ENDOR studies of VO2+: probing protein-metal ion interactions in nephrocalcin. Cell Mol Biol (Noisy-le-grand) (2000) 0.79
ENDOR structural characterization of a catalytically competent acylenzyme reaction intermediate of wild-type TEM-1 beta-lactamase confirms glutamate-166 as the base catalyst. Biochemistry (2001) 0.78
Crystallographic and chemical studies on cytosolic aspartate aminotransferase. Prog Clin Biol Res (1984) 0.78
Polarized single-crystal absorption spectrum of cytosine monohydrate. J Am Chem Soc (1971) 0.77
The pH variation of steady-state kinetic parameters of site-specific Co(2+)-reconstituted liver alcohol dehydrogenase. A mechanistic probe for the assignment of metal-linked ionizations. J Biol Chem (1991) 0.76
The second derivative electronic absorption spectrum of cytochrome c oxidase in the Soret region. Biophys J (1999) 0.75
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Cryostat for enzymology in the subzero temperature range. Rev Sci Instrum (1978) 0.75