William Eaton

Q: What Schools Are Affiliated With William Eaton

William Eaton is affiliated with the following schools: University of California, San Francisco, University of Granada, University of Pennsylvania, University of Potsdam, University of Maryland, College Park, University of California, Berkeley, University of Parma, University of Wyoming, University of Michigan, Wayne State University

William Eaton 's AcademicInfluence.com Rankings

William Eaton

Physics

#3798

World Rank

#5324

Historical Rank

#1338

USA Rank

Biophysics

#166

World Rank

#176

Historical Rank

#38

USA Rank

physics Degrees

Download Badge

Physics

William Eaton 's Degrees

PhD Biophysics University of California, Berkeley
Bachelors Physics University of California, Berkeley

Why Is William Eaton Influential?

(Suggest an Edit or Addition)

According to Wikipedia, William Allen Eaton is a biophysical chemist who is a NIH Distinguished Investigator, Chief of the Section on Biophysical Chemistry, and Chief of the Laboratory of Chemical Physics at the National Institute of Diabetes and Digestive and Kidney Diseases, one of the 20 Institutes of the United States National Institutes of Health.

(See a Problem?)

William Eaton 's Published Works

Number of citations in a given year to any of this author's works

Total number of citations to an author for the works they published in a given year. This highlights publication of the most important work(s) by the author

Published Works

Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy (2002) (802)
Folding dynamics and mechanism of β-hairpin formation (1997) (773)
The protein folding 'speed limit'. (2004) (755)
Protein folding studied by single-molecule FRET. (2008) (610)
A simple model for calculating the kinetics of protein folding from three-dimensional structures. (1999) (564)
Sickle cell hemoglobin polymerization. (1990) (556)
Native contacts determine protein folding mechanisms in atomistic simulations (2013) (459)
The role of solvent viscosity in the dynamics of protein conformational changes. (1992) (450)
Kinetics and mechanism of deoxyhemoglobin S gelation: a new approach to understanding sickle cell disease. (1974) (434)
Fast kinetics and mechanisms in protein folding. (2000) (432)
Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism. (1985) (423)
Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence. (2005) (387)
Hemoglobin S gelation and sickle cell disease. (1987) (372)
Single-Molecule Fluorescence Experiments Determine Protein Folding Transition Path Times (2012) (346)
Measuring the rate of intramolecular contact formation in polypeptides. (2000) (343)
Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. (1996) (338)
Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations (2007) (332)
Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model. (1997) (307)
Single-Molecule Measurement of Protein Folding Kinetics (2003) (303)
Fast events in protein folding initiated by nanosecond laser photolysis. (1993) (276)
Is cooperative oxygen binding by hemoglobin really understood? (1999) (275)
Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering. (1999) (255)
Experimental determination of upper bound for transition path times in protein folding from single-molecule photon-by-photon trajectories (2009) (253)
Kinetics of sickle hemoglobin polymerization. I. Studies using temperature-jump and laser photolysis techniques. (1985) (252)
Submillisecond protein folding kinetics studied by ultrarapid mixing. (1997) (233)
Sub-microsecond protein folding. (2006) (223)
Experimental tests of villin subdomain folding simulations. (2003) (209)
Molecular dynamics simulations of cooling in laser-excited heme proteins. (1986) (206)
High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein. (2005) (204)
Geminate recombination of carbon monoxide to myoglobin. (1983) (199)
Delay time of hemoglobin S polymerization prevents most cells from sickling in vivo. (1987) (199)
Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism. (1980) (195)
Optical spectra of oxy- and deoxyhemoglobin (1978) (188)
A multiparameter analysis of sickle erythrocytes in patients undergoing hydroxyurea therapy. (1996) (184)
A statistical mechanical model for β-hairpin kinetics (1998) (182)
Effect of flexibility and cis residues in single-molecule FRET studies of polyproline (2007) (181)
Single molecule fluorescence probes dynamics of barrier crossing (2013) (179)
Supersaturation in sickle cell hemoglobin solutions. (1976) (178)
Submillisecond kinetics of protein folding. (1997) (176)
Conformational relaxation and ligand binding in myoglobin. (1994) (174)
Effects of chain stiffness on the dynamics of loop formation in polypeptides. Appendix: Testing a 1-dimensional diffusion model for peptide dynamics (2002) (172)
Structural origin of slow diffusion in protein folding (2015) (166)
Polarized absorption and linear dichroism spectroscopy of hemoglobin. (1981) (166)
Nanosecond absorption spectroscopy of hemoglobin: elementary processes in kinetic cooperativity. (1983) (162)
Folding dynamics and mechanism of beta-hairpin formation. (1997) (158)
Electronic spectrum of single crystals of ferricytochrome-c. (1967) (151)
Treating sickle cell disease by targeting HbS polymerization. (2017) (150)
Measuring internal friction of an ultrafast-folding protein (2008) (148)
Single-crystal spectra of ferrimyoglobin complexes in polarized light. (1968) (144)
Letter: Origin of the anomalous Soret spectra of carboxycytochrome P-450. (1976) (140)
Chemical, physical, and theoretical kinetics of an ultrafast folding protein (2008) (136)
A tertiary two-state allosteric model for hemoglobin. (2002) (136)
Requirements for therapeutic inhibition of sickle haemoglobin gelation (1978) (135)
Thermodynamics of gelation of sickle cell deoxyhemoglobin. (1977) (130)
Kinetics and Dynamics of Loops, α-Helices, β-Hairpins, and Fast-Folding Proteins (1998) (129)
Gelation of sickle cell hemoglobin in mixtures with normal adult and fetal hemoglobins. (1979) (129)
Thermodynamic aspects of the potassium hexacyano-ferrate(III)-(II) system. II. Reduction potential (1967) (123)
Editorial: Delay time of gelation: a possible determinant of clinical severity in sickle cell disease (1976) (121)
Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect (1991) (112)
Oxygen binding by single crystals of hemoglobin. (1993) (110)
Solution structure of the ESCRT-I complex by small-angle X-ray scattering, EPR, and FRET spectroscopy (2011) (110)
Evolution of allosteric models for hemoglobin (2007) (108)
Molecular and cellular pathogenesis of hemoglobin SC disease. (1982) (107)
Fast events in protein folding. (1996) (105)
Oxygen binding by sickle cell hemoglobin polymers. (1982) (101)
New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels. (2004) (100)
Spectroscopic studies of oxy- and carbonmonoxyhemoglobin after pulsed optical excitation. (1978) (99)
The biophysics of sickle cell hydroxyurea therapy. (1995) (97)
Two-state expansion and collapse of a polypeptide. (2000) (95)
Can a two-state MWC allosteric model explain hemoglobin kinetics? (1997) (91)
Rate of Intrachain Diffusion of Unfolded Cytochrome c (1997) (91)
Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein. (2011) (91)
Thermodynamic aspects of the potassium hexacyanoferrate(III)-(II) system. I. Ion association. (1967) (90)
The relationship between coding sequences and function in haemoglobin (1980) (90)
Linear dichroism of biological chromophores. (1976) (89)
Kinetics of sickle haemoglobin polymerization in single red cells (1982) (88)
Solution structure of the ESCRT-I and -II supercomplex: implications for membrane budding and scission. (2012) (87)
Searching for "downhill scenarios" in protein folding. (1999) (86)
Comparing a simple theoretical model for protein folding with all-atom molecular dynamics simulations (2013) (85)
Understanding the shape of sickled red cells. (2005) (83)
Effects of denaturants on the dynamics of loop formation in polypeptides. (2006) (82)
Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication. (1985) (79)
Combinatorial modeling of protein folding kinetics: free energy profiles and rates (2004) (79)
Chemical physics of protein folding (1998) (78)
Protein folding transition path times from single molecule FRET. (2018) (75)
Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data. (2008) (74)
Molecular dynamics simulation of photodissociation of carbon monoxide from hemoglobin. (1985) (74)
GEMINATE REBINDING AND CONFORMATIONAL DYNAMICS OF MYOGLOBIN EMBEDDED IN A GLASS AT ROOM TEMPERATURE (1996) (68)
Determination of ultrafast protein folding rates from loop formation dynamics. (2005) (67)
Calorimetric and optical characterization of sickle cell hemoglobin gelation. (1975) (67)
Application of linear free energy relations to protein conformational changes: the quaternary structural change of hemoglobin. (1991) (66)
Time-resolved optical spectroscopy and structural dynamics following photodissociation of carbonmonoxyhemoglobin. (1988) (62)
A statistical mechanical model for beta-hairpin kinetics. (1998) (61)
Polarized single-crystal absorption spectrum of 1-methyluracil. (1970) (61)
Distinguishing between protein dynamics and dye photophysics in single-molecule FRET experiments. (2010) (59)
Speed of intersubunit communication in proteins. (1992) (58)
Nonexponential structural relaxations in proteins (1996) (58)
Making connections between ultrafast protein folding kinetics and molecular dynamics simulations (2011) (58)
Folding and Aggregation Kinetics of a β-Hairpin† (2006) (58)
Two-state expansion and collapse of a polypeptide. (2000) (57)
Dynamics of intramolecular contact formation in polypeptides: distance dependence of quenching rates in a room-temperature glass. (2001) (56)
Kinetics of intramolecular contact formation in a denatured protein. (2003) (55)
The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin. (1988) (54)
Allosteric effectors do not alter the oxygen affinity of hemoglobin crystals (1997) (50)
Structure of hemoglobin S fibers: optical determination of the molecular orientation in sickled erythrocytes. (1973) (49)
Infrared Magnetic Circular Dichroism in the Study of Metalloproteins (1973) (48)
Testing Landscape Theory for Biomolecular Processes with Single Molecule Fluorescence Spectroscopy. (2015) (47)
POLARIZED SINGLE CRYSTAL ABSORPTION SPECTRA OF CARBOXY‐ AND OXYHEMOGLOBIN (1973) (46)
Measuring dynamic flexibility of the coil state of a helix-forming peptide. (2002) (44)
Evidence for a partially structured state of the amylin monomer. (2009) (44)
Experimental basis for a new allosteric model for multisubunit proteins (2014) (43)
Comparison of sickle cell hemoglobin gelation kinetics measured by NMR and optical methods. (1976) (43)
Simulation of the kinetics of ligand binding to a protein by molecular dynamics: geminate rebinding of nitric oxide to myoglobin. (1993) (43)
Dynamics of Intramolecular Contact Formation in Polypeptides (2001) (41)
Sedimentation studies on human amylin fail to detect low-molecular-weight oligomers. (2008) (41)
Polarized single-crystal absorption spectrum of cytosine monohydrate. (1971) (41)
Near-infrared absorption and circular dichroism spectra of ferrocytochrome c: d-d transitions. (1969) (41)
Relaxation rate for an ultrafast folding protein is independent of chemical denaturant concentration. (2007) (40)
Near-infrared circular dichroism of an iron-sulfur protein. D leads to d transitions in rubredoxin. (1970) (39)
Measuring ultrafast protein folding rates from photon-by-photon analysis of single molecule fluorescence trajectories. (2013) (39)
Theory, simulations, and experiments show that proteins fold by multiple pathways (2017) (38)
Optical Triggers of Protein Folding (1996) (38)
Kinetic assay shows that increasing red cell volume could be a treatment for sickle cell disease (2017) (38)
Physics of virus transmission by speaking droplets (2020) (37)
Linus Pauling and sickle cell disease. (2002) (37)
Optical spectra and electronic structure of flavine mononucleotide in flavodoxin crystals. (1975) (36)
Optically Detected Conformational Changes in Haemoglobin Single Crystals (1974) (35)
Photoselection in polarized photolysis experiments on heme proteins. (1993) (33)
Picosecond transient absorption study of photodissociated carboxy hemoglobin and myoglobin. (1988) (33)
Treatment of sickle cell disease by increasing oxygen affinity of hemoglobin. (2021) (33)
Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models. (2015) (32)
Tetrahedral iron in the active center of plant ferredoxins and beef adrenodoxin. (1971) (32)
Dynamics of the quaternary conformational change in trout hemoglobin. (1991) (32)
Treating sickle cell anemia (2020) (28)
Oxygen binding by single crystals of hemoglobin: the problem of cooperativity and inequivalence of alpha and beta subunits. (1996) (26)
Editorial: Delay time of gelation: a possible determinant of clinical severity in sickle cell disease. (1976) (26)
Universality of supersaturation in protein-fiber formation (2016) (23)
Hemoglobin S polymerization and sickle cell disease: A retrospective on the occasion of the 70th anniversary of Pauling's Science paper (2019) (22)
The physics of protein folding (1999) (22)
Charge-transfer optical spectra, electron paramagnetic resonance, and redox potentials of cytochromes (1984) (20)
Protein Structure: Nanosecond Crystallographic Snapshots of Protein Structural Changes (1996) (20)
Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease (2020) (17)
Estimating computational limits on theoretical descriptions of biological cells (2021) (17)
Mixing Nanoliters in Microseconds (1998) (17)
Folding and aggregation kinetics of a beta-hairpin. (2006) (15)
CHAPTER 3 – The Iron-Sulfur Complex in Rubredoxin (1973) (15)
Modern Kinetics and Mechanism of Protein Folding: A Retrospective (2021) (15)
A Phase 1 Dose Escalation Study of the Pyruvate Kinase Activator Mitapivat (AG-348) in Sickle Cell Disease. (2022) (13)
A crystallographic study of deoxy cobalt (II) mesoporphyrin IX myoglobin. (1975) (12)
Voxelotor treatment of a patient with sickle cell disease and very severe anemia (2019) (10)
SUCCESSES AND FAILURES OF A SIMPLE NUCLEATION THEORY FOR SICKLE CELL HEMOGLOBIN GELATION (1978) (9)
Current Perspectives on the Kinetics of Hemoglobin S Gelation (1989) (9)
MWC allosteric model explains unusual hemoglobin-oxygen binding curves from sickle cell drug binding (2021) (7)
corrigendum: Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy (2003) (7)
Interactions of an Anti-Sickling Drug with Hemoglobin in Red Blood Cells from a Patient with Sickle Cell Anemia. (2019) (7)
Impact of hemoglobin biophysical studies on molecular pathogenesis and drug therapy for sickle cell disease. (2021) (6)
Viewpoint: Transition Path Times for DNA and RNA Folding from Force Spectroscopy (2012) (6)
Comments on the physics and chemistry of trehalose as a storage medium for hemoglobin-based blood substitutes: "from Kramers Theory to the Battlefield". (1995) (6)
Phase 1 Multiple Ascending Dose Study of Safety, Tolerability, and Pharmacokinetics/Pharmacodynamics of Mitapivat (AG-348) in Subjects with Sickle Cell Disease (2020) (5)
Mitapivat (AG-348) Demonstrates Safety, Tolerability, and Improvements in Anemia, Hemolysis, Oxygen Affinity, and Hemoglobin S Polymerization Kinetics in Adults with Sickle Cell Disease: A Phase 1 Dose Escalation Study (2021) (4)
Nanosecond crystallographic snapshots of protein structural changes. (1996) (3)
Impact of Conformational Substates and Energy Landscapes on Understanding Hemoglobin Kinetics and Function (2021) (3)
HEMOGLOBIN S POLYMERIZATION IN THE PHOTOSTATIONARY STATE (1978) (3)
Thermodynamic aspects of the potassium hexacyanoferrate(3)-(2) system. II. Reduction potential. (1967) (3)
Folding and binding (1991) (3)
Phenotypic screening of the ReFRAME drug repurposing library to discover new drugs for treating sickle cell disease (2022) (2)
Robin Main Hochstrasser (1931–2013), giant of physical chemistry (2013) (2)
A retrospective on statistical mechanical models for hemoglobin allostery (2022) (2)
Oxygen binding by single crystals of hemoglobin: The problem of cooperativity and inequivalence of alpha and beta subunits (1996) (2)
Scientific Contributions of Robin M. Hochstrasser (1996) (1)
Single-Molecule FRET Shows Folding Transition Path Time for All-Alpha Protein Slowed by Internal Friction (2013) (1)
Autobiography of William A. Eaton. (2018) (1)
Structural Origin of Landscape Roughness in Protein Folding from Single-Molecule FRET and All-Atom Molecular Dynamics Simulations (2015) (1)
A Simple Model for Protein Folding (2009) (1)
Mitapivat increases ATP and decreases oxidative stress and erythrocyte mitochondria retention in a SCD mouse model. (2022) (1)
Single Molecule FRET Studies of DNA Hairpin Folding (2014) (1)
Proceedings of the first national symposium on sickle cell disease (1974) (1)
Oxygen Binding and the Gelation of Sickle Cell Hemoglobin (1981) (1)
NEAR INFRARED CIRCULAR DICHROISM: d → d TRANSITIONS IN HEMOPROTEINS (1971) (1)
Dynamics of Structural Changes in Hemoglobin (1987) (1)
Figure 5, [Schematic structures of monomeric λ repressor (left) and muscle acyl phosphatase (right).]. (2002) (0)
Colleagues of William A. Eaton. (2018) (0)
Figure 3, [Processes contributing to temperature-dependent changes...]. (2002) (0)
After Dinner Program: To Honor Max Perutz (1982) (0)
Measuring Sub-Microsceond Protein Folding Kinetics with Independent Probes (2011) (0)
Single Molecule Fluorescence Studies of Transition Paths in DNA Hairpin Folding (2016) (0)
Chicken villin subdomain HP-35, N68H, pH6.7 (2005) (0)
Chicken villin subdomain HP-35, K65(NLE), N68H, pH7.0 (2005) (0)
Photon-By-Photon Analysis of Single Molecule Fluorescence Trajectories of a Fast Folding Protein (2010) (0)
POLARISIERTES EINKRISTALL-ABSORPTIONSSPEKTRUM VON 1-METHYL-URACIL (1970) (0)
Max Delbruck Prize in Biological Physics Lecture: Single-molecule protein folding and transition paths (2012) (0)
Chicken villin subdomain HP-35, K65(NLE), N68H, pH5.1 (2005) (0)
Application oflinear freeenergy relations toprotein conformational changes: Thequaternary structural change ofhemoglobin (kinetics/dynamics/transition state theory/reaction path/allostery) (1991) (0)
Publications of William A. Eaton. (2018) (0)
Figure 6, [A simple statistical model for...]. (2002) (0)
The ever changing world of ( hemo ) globins (2008) (0)
Polarized absorption spectra of P 450(cam) single crystals (1975) (0)
The problem of describing gelation in vivo. (1987) (0)
Robin Hochstrasser Biographical Memoir (2018) (0)
The Biophysical Basis of Drug Therapy for Sickle Cell Disease (2018) (0)
Photon-by-photon trajectories of single protein molecules folding and unfolding (2010) (0)
Complementary DNA for 12-Kilodalton B Cell Growth Factor : Misassigned (2006) (0)
The Conquest of the Soudan: Gordon Avenged (2009) (0)
Single Molecule Photon Trajectories and Transition Paths in Protein Folding (2010) (0)
Supersaturation in sickle cell hemoglobin solutions * ( sickle cell disease / hemoglobin S gelation / protein self-assembly / nucleation kinetics / protein solubility ) (2003) (0)
Mutations in the Hemoglobin Binding Domain of Band 3 Perturb Cellular Metabolism and Alter the Sickling of SS Erythrocytes (2021) (0)
NEAR INFRARED CIRCULAR DICHROISM: $d \rightarrow d$ TRANSITIONS IN HEMOPROTEINS. (1969) (0)
Figure 2, [Using long-lived triplet states to...]. (2002) (0)
Extreme Mechanical Stability In Polyglutamine Chains Identified Using Single Molecule Force-clamp Spectroscopy (2009) (0)
Contributory presentations/posters (1999) (0)
Chicken villin subdomain HP-35, K65(NLE), N68H, K70(NLE), PH9 (2006) (0)
Molecular Dynamics Study of Vibrational Cooling in Optically Excited Hemeproteins (1986) (0)
Chicken villin subdomain HP-35, N68H, pH6.4 (2005) (0)
Collapse Of Rat And Human Amylin From Nanosecond-resolved Intramolecular Contact Formation (2009) (0)
Molecular dynamics simulations of cooling in laser-excited heme proteins ( picosecond spectroscopy / intramolecular vibrational relaxation / Raman spectroscopy / hemoglobin / myoglobin ) (0)
Figure 4, [Model for formation of β-hairpin...]. (2002) (0)
TheRole ofSolvent Viscosity intheDynamics of Protein Conformational Changes (1993) (0)
Symposia lectures (2007) (0)
Tribute to Peter G. Wolynes. (2013) (0)
Protein Folding Transition Paths: Single Molecule Experiments, Theory and Simulations (2015) (0)
Sickle Cell Hemoglobin Polymers Bind Oxygen Noncooperatively (1982) (0)
Photon-By-Photon Analysis of Single Molecule Fluorescence Trajectories Determines an Upper Bound for the Transition Path Time in Protein Folding (2011) (0)
Kinetics of an ultrafast folding protein analyzed with a free energy surface model (2005) (0)
spectroscopy/picosecond kinetics) (1985) (0)
Measurement of Single Molecule Folding/unfolding Trajectories (2009) (0)
[Microspectrophotometry in the study of physiological and pathological events in erythrocytes]. (1983) (0)
Dynamics of Vibrational Populations in Optically Pumped Hemeproteins (1986) (0)
Drug discovery by a basic research scientist (2022) (0)
1999 XIII International Biophysics Congress 19-24 September 1999 New Delhi Abstracts Suppl (2016) (0)
A tribute to Attila Szabo. (2008) (0)
Are there common themes in the function, energy landscape, and dynamics of Proteins? (1999) (0)
Measurement of Average Transition-Path Time for Protein Folding in Single Molecule FRET Experiments (2012) (0)
POLARISIERTES EINKRISTALL-ABSORPTIONSSPEKTRUM VON CYTOSINMONOHYDRAT (1971) (0)
Figure 1, [Initiating the folding of reduced...]. (2002) (0)
Molecular Dynamics Simulation of Ligand Photodissociation from Hemoglobin (1987) (0)
Hemoglobin S Polymerization Can be Inhibited By Alterations in Erythrocyte Glycolysis (2019) (0)
Kinetics of Intramolecular Contact Formation in Unfolded Proteins (2005) (0)
Abbreviated Curriculum Vitae of William A. Eaton. (2018) (0)
Molecular and cellular pathogenesis of hemoglobin SC disease ( hemoglobinopathies / sickle cell disease / hemoglobins S and C / protein polymerization / erythrocyte density ) (0)
Supporting Online Material for Single Molecule Measurement of Protein Folding Kinetics (2003) (0)

This paper list is powered by the following services:

Other Resources About William Eaton

What Schools Are Affiliated With William Eaton ?

William Eaton is affiliated with the following schools:

William Eaton 's Academic­Influence.com Rankings