Published in Nature on April 17, 1975
Substrate-induced deactivation of penicillinases. Studies of beta-lactamase I by hydrogen exchange. Biochem J (1977) 1.32
NMR analysis of the alphaIIb beta3 cytoplasmic interaction suggests a mechanism for integrin regulation. Proc Natl Acad Sci U S A (2010) 1.16
Comparison of bacterial and animal rhodopsins by hydrogen exchange studies. Nature (1977) 0.88
Light-regulated permeability of rhodopsin:egg phosphatidylcholine recombinant membranes. Proc Natl Acad Sci U S A (1977) 0.81
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
Hydrogen exchange. Annu Rev Biochem (1972) 3.31
Isotope effects in peptide group hydrogen exchange. Proteins (1993) 3.21
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
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
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
Biochemistry without oxygen. Anal Biochem (1987) 1.77
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
Characterization of a seventh different subunit of beef heart cytochrome c oxidase. Similarities between the beef heart enzyme and that from other species. Biochemistry (1976) 1.56
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
Ultrafast signals in protein folding and the polypeptide contracted state. Proc Natl Acad Sci U S A (1997) 1.35
Hydrogen exchange study of some polynucleotides and transfer RNA. J Mol Biol (1972) 1.27
Quenching of room temperature protein phosphorescence by added small molecules. Biochemistry (1988) 1.27
Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence. Biochemistry (1983) 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
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
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
Hydrogen exchange of lysozyme powders. Hydration dependence of internal motions. Biochemistry (1985) 1.10
Labeling of cytochrome c oxidase with [35S]diazobenzenesulfonate. Orientation of this electron transfer complex in the inner mitochondrial membrane. Biochemistry (1979) 1.09
Measuring the conformational stability of a protein by hydrogen exchange. Methods Mol Biol (2001) 1.08
Infrared spectroscopic study of photoreceptor membrane and purple membrane. Protein secondary structure and hydrogen deuterium exchange. J Biol Chem (1986) 1.05
Two-dimensional 1H NMR studies of cytochrome c: assignment of the N-terminal helix. Biochemistry (1986) 1.03
Individual breathing reactions measured by functional labeling and hydrogen exchange methods. Methods Enzymol (1986) 1.00
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
Allosteric energy at the hemoglobin beta chain C terminus studied by hydrogen exchange. J Mol Biol (1988) 0.95
Protein complexes studied by NMR spectroscopy. Curr Opin Biotechnol (1996) 0.95
Hydrogen exchange. Nat Struct Biol (2001) 0.95
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
Hydrogen-exchange measurements on Escherichia coli transfer ribonucleic acid before, after, and during its aminoacylation. Biochemistry (1969) 0.93
Measurement of the free and the H-bonded amides of myoglobin. J Mol Biol (1969) 0.93
Native collagen has a two-bonded structure. J Mol Biol (1974) 0.93
The loop problem in proteins: a Monte Carlo simulated annealing approach. Biopolymers (1993) 0.93
Salt, phosphate and the Bohr effect at the hemoglobin beta chain C terminus studied by hydrogen exchange. J Mol Biol (1988) 0.92
Energetic components of the allosteric machinery in hemoglobin measured by hydrogen exchange. J Mol Biol (1998) 0.92
Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c. Biophys J (1990) 0.92
Long-range electron exchange measured in proteins by quenching of tryptophan phosphorescence. Proc Natl Acad Sci U S A (1990) 0.91
Signal transmission between subunits in the hemoglobin T-state. J Mol Biol (1998) 0.91
Hydrogen exchange studies of respiratory proteins. 3. Structural and free energy changes in hemoglobin by use of a difference method. J Biol Chem (1973) 0.90
Structural dynamics in an electron-transfer complex. Nat Struct Biol (1994) 0.89
Comparison of bacterial and animal rhodopsins by hydrogen exchange studies. Nature (1977) 0.88
A high energy structure change in hemoglobin studied by difference hydrogen exchange. J Biol Chem (1980) 0.88
Two-dimensional 1H NMR studies of cytochrome c. Biochemistry (1985) 0.88
Mixed gelation theory. Kinetics, equilibrium and gel incorporation in sickle hemoglobin mixtures. J Mol Biol (1979) 0.87
How much is a stabilizing bond worth? Trends Biochem Sci (1994) 0.85
Cross-linking of dark-adapted frog photoreceptor disk membranes. Evidence for monomeric rhodopsin. Biophys J (1985) 0.85
Truncated desmin in PtK2 cells induces desmin-vimentin-cytokeratin coprecipitation, involution of intermediate filament networks, and nuclear fragmentation: a model for many degenerative diseases. Proc Natl Acad Sci U S A (1994) 0.84
Interpretation of data on sequential labeling of growing polypeptides. Biochem Biophys Res Commun (1965) 0.84
Hydrogen exchange study of membrane-bound rhodopsin. I. Protein structure. J Biol Chem (1977) 0.84
Internal protein motions, concentrated glycerol, and hydrogen exchange studied in myoglobin. Biochemistry (1985) 0.83
Re-examination of rhodopsin structure by hydrogen exchange. J Biol Chem (1982) 0.83
Transient dichroism in photoreceptor membranes indicates that stable oligomers of rhodopsin do not form during excitation. Biophys J (1985) 0.83
Hydrogen-tritium exchange survey of allosteric effects in hemoglobin. Biochemistry (1987) 0.82
Native-state HX. Trends Biochem Sci (1998) 0.81
Measurement of protein structure change in active muscle by hydrogen-tritium exchange. Biophys Chem (1996) 0.81
Premelting and the hydrogen-exchange open state in synthetic RNA duplexes. Biopolymers (1984) 0.81
Hydrogen exchange studies of respiratory proteins. IV. A new, ligand-responsive class in hemoglobin. J Biol Chem (1974) 0.80
Glycation of calmodulin: chemistry and structural and functional consequences. Biochemistry (1989) 0.80
Hydrogen exchange studies on ribosomes. Biochemistry (1967) 0.79
Salt-dependent structure change and ion binding in cytochrome c studied by two-dimensional proton NMR. Biochemistry (1990) 0.79