Serge N. Timasheff

Serge N. Timasheff's AcademicInfluence.com Rankings

Serge N. Timasheff

Chemistry

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#1702

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chemistry Degrees

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Chemistry

Serge N. Timasheff's Degrees

PhD Chemistry University of California, Berkeley

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Serge N. Timasheff'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

Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. (1981) (1105)
Stabilization of protein structure by sugars. (1982) (1002)
The stabilization of proteins by sucrose. (1981) (986)
The control of protein stability and association by weak interactions with water: how do solvents affect these processes? (1993) (955)
The stabilization of proteins by osmolytes. (1985) (917)
Structure and stability of biological macromolecules (1969) (683)
Preferential interactions of proteins with salts in concentrated solutions. (1982) (634)
Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding. (1984) (584)
Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components (2002) (562)
Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. (1998) (553)
Thermodynamic and kinetic examination of protein stabilization by glycerol. (1981) (445)
Protein hydration, thermodynamic binding, and preferential hydration. (2002) (436)
Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects. (2007) (423)
Mechanism of poly(ethylene glycol) interaction with proteins. (1985) (404)
The thermodynamic mechanism of protein stabilization by trehalose. (1997) (340)
Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein. (1994) (334)
Theory of protein solubility. (1985) (316)
Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols (1992) (314)
Infrared spectra and protein conformations in aqueous solutions. I. The amide I band in H2O and D2O solutions. (1967) (312)
Preferential interactions of proteins with solvent components in aqueous amino acid solutions. (1983) (307)
Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. (1974) (303)
In vitro reconstitution of calf brain microtubules: effects of solution variables. (1977) (302)
Contribution of the surface free energy perturbation to protein-solvent interactions. (1994) (261)
Water as ligand: preferential binding and exclusion of denaturants in protein unfolding. (1992) (255)
Protein precipitation and denaturation by dimethyl sulfoxide. (2007) (236)
Aggregation of microtubule subunit protein. Effects of divalent cations, colchicine and vinblastine. (1970) (223)
Why preferential hydration does not always stabilize the native structure of globular proteins. (1990) (219)
Mechanism of the stabilization of ribonuclease a by sorbitol: Preferential hydration is greater for the denatured than for the native protein (1997) (219)
On the role of surface tension in the stabilization of globular proteins (1996) (216)
The reconstitution of microtubules from purified calf brain tubulin. (1975) (205)
The chemical characterization of calf brain microtubule protein subunits. (1973) (205)
Protein stabilization and destabilization by guanidinium salts. (1984) (200)
The interaction of proteins with hydroxyapatite. III. Mechanism. (1984) (193)
Preferential interactions determine protein solubility in three-component solutions: the magnesium chloride system (1990) (180)
Cold depolymerization of microtubules to double rings: geometric stabilization of assemblies. (1989) (174)
Molecular Interactions in β-Lactoglobulin. II. Ultracentrifugal and Electrophoretic Studies of the Association of β-Lactoglobulin below its Isoelectric Point2 (1960) (164)
Magnesium-induced self-association of calf brain tubulin. I. Stoichiometry. (1975) (161)
In vitro assembly of cytoplasmic microtubules. (1980) (159)
Infrared spectra and protein conformations in aqueous solutions. II. Survey of globular proteins. (1967) (152)
Interactions of proteins with solvent components in 8 M urea. (1981) (149)
Protein-solvent interactions and protein conformation (1970) (131)
Interaction of Vinblastine with Calf Brain Microtubule protein. (1975) (130)
Measurements of preferential solvent interactions by densimetric techniques. (1979) (130)
Preferential binding of solvent components to proteins in mixed water--organic solvent systems. (1968) (130)
Mechanism of protein precipitation and stabilization by co-solvents (1988) (128)
Preferential interactions of urea with lysozyme and their linkage to protein denaturation. (2003) (125)
Conformational states of tubulin liganded to colchicine, tropolone methyl ether, and podophyllotoxin. (1982) (124)
Molecular Interactions in β-Lactoglobulin. IV. The Dissociation of β-Lactoglobulin below pH 3.52 (1960) (123)
Interaction of tubulin with single ring analogues of colchicine. (1982) (121)
The circular dichroism of polypeptide films. (1968) (120)
Molecular Interactions in β-Lactoglobulin. III. Light Scattering Investigation of the Stoichiometry of the Association between pH 3.7 and 5.22 (1960) (117)
Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5.8. (1978) (114)
Dimerization of alpha-chymotrypsin. I. pH dependence in the acid region. (1971) (114)
Magnesium-induced self-association of calf brain tubulin. II. Thermodynamics. (1975) (114)
Interaction of calf brain tubulin with glycerol. (1981) (110)
The mechanism of action of Na glutamate, lysine HCl, and piperazine-N,N'-bis(2-ethanesulfonic acid) in the stabilization of tubulin and microtubule formation. (1984) (109)
A Physicochemical Basis for the Selection of Osmolytes by Nature (1992) (108)
Subunits in biological systems (1971) (107)
The interaction of tubulin and other proteins with structure-stabilizing solvents☆ (1976) (105)
In disperse solution, "osmotic stress" is a restricted case of preferential interactions. (1998) (105)
Circular dichroism of polypeptide and protein conformations. Film studies. (1970) (102)
Dimerization of alpha-chymotrypsin. II. Ionic strength and temperature dependence. (1971) (99)
GDP state of tubulin: stabilization of double rings. (1986) (96)
Tubulin bound to colchicine forms polymers different from microtubules. (1982) (96)
Interaction of tubulin with bifunctional colchicine analogues: an equilibrium study. (1984) (94)
Molecular Interactions in β-Lactoglobulin. V. the Association of the Genetic Species of β-Lactoglobulin below the Isoelectric Point2 (1961) (90)
Conformation of proteins. (1967) (89)
The circulation dichroism of variants of beta-lactoglobulin. (1967) (87)
The interaction of beta-lactoglobulin with solvent components in mixed water-organic solvent systems. (1968) (86)
The measurement of cooperative protein self-assembly by turbidity and other techniques. (1986) (85)
Role of the colchicine ring A and its methoxy groups in the binding to tubulin and microtubule inhibition. (1998) (82)
Molecular Interactions in β-Lactoglobulin. VI. the Dissociation of the Genetic Species of β-Lactoglobulin at Acid pH's2 (1961) (81)
Interaction of vinblastine with calf brain tubulin: multiple equilibria. (1986) (80)
Stoichiometry of the vinblastine-induced self-association of calf brain tubulin. (1980) (79)
Preferential solvation of bovine serum albumin in aqueous guanidine hydrochloride. (1967) (78)
Solvent stabilization of protein structure. (1995) (77)
The Optical Rotatory Dispersion of the β-Lactoglobulins (1966) (76)
In vitro reconstitution of calf brain microtubules: effects of macromolecules. (1978) (74)
The state of amino acid residues in β-lactoglobulin (1969) (71)
Infrared Spectra and Protein Conformations in Aqueous Solutions (1967) (71)
Abnormal solubility behavior of .beta.-lactoglobulin: salting-in by glycine and sodium chloride (1987) (70)
Thermodynamic linkage between tubulin self-association and the binding of vinblastine. (1980) (70)
Molecular interactions in beta-lactoglobulin. X. The stoichiometry of the beta-lactoglobulin mixed tetramerization. (1966) (64)
Molecular Interactions in β-Lactoglobulin. VIII. Small-Angle X-Ray Scattering Investigation of the Geometry of β-Lactoglobulin A Tetramerization (1964) (63)
Temperature dependence of the hydrogen ion equilibria in poly(riboadenylic acid) (1968) (63)
The calculation of partial specific volumes of proteins in guanidine hydrochloride. (1974) (63)
Infrared Investigation of the Secondary Structure of β-Lactoglobulins (1966) (62)
Polymerization of the tubulin-colchicine complex: relation to microtubule assembly. (1983) (61)
Hydrogen ion equilibria of the genetic variants of bovine β-lactoglobulin (1967) (60)
Temperature dependence of the preferential interactions of ribonuclease a in aqueous co‐solvent systems: Thermodynamic analysis (1997) (60)
Diffraction methods for biological macromolecules (1985) (59)
Investigations on Proteins and Polymers. IV.1 Critical Phenomena in Polyvinyl Alcohol-Acetate Copolymer Solutions (1951) (58)
Physical-chemical study of daunomycin-tubulin interactions. (1977) (56)
Preferential interactions determine protein solubility in three-component solutions: the MgCl2 system. (1990) (55)
Light Scattering Investigation of Charge Fluctuations in Isoionic Serum Albumin Solutions1 (1957) (54)
Fine structure of proteins and nucleic acids (1970) (53)
The extrapolation of light-scattering data to zero concentration. (1959) (52)
Some observations of the sedimentation of chicken heart glyceraldehyde 3-phosphate dehydrogenase. (1970) (52)
In vitro vinblastine-induced tubulin paracrystals. (1982) (52)
Conformational transitions of bovine beta-lactoglobulins A, B, and C. (1966) (51)
Thermodynamic binding and site occupancy in the light of the Schellman exchange concept. (2002) (49)
Linkages between the effects of taxol, colchicine, and GTP on tubulin polymerization. (1988) (49)
Turbidity as a criterion of coagulation (1966) (48)
Interactions of tubulin with guanylyl-(beta-gamma-methylene)diphosphonate. Formation and assembly of a stoichiometric complex. (1990) (47)
Solvent effects on protein stability: Current Opinion in Structural Biology 1992, 2:35…-39 (1992) (46)
Polarized fluorescence decay curves for beta-lactoglobulin A in various states of association. (1969) (46)
Conformational study of calf brain tubulin. (1978) (45)
The calculation of partial specific volumes of proteins in 6 M guanidine hydrochloride. (1979) (45)
Molecular Interactions in β-Lactoglobulin. IX. Optical Rotatory Dispersion of the Genetic Variants in Different States of Association2 (1964) (43)
Optical rotatory dispersion and circular dichroism properties of yeast mitochondrial DNA's. (1970) (43)
Roles of colchicine rings B and C in the binding process to tubulin. (1989) (42)
The structure of high molecular weight ribonucleic acid in solution. A smallangle x-ray scattering study. (1961) (42)
Mechanism of interaction of vinca alkaloids with tubulin: catharanthine and vindoline. (1991) (42)
Modulation of recombinant human prostate-specific antigen: activation by Hofmeister salts and inhibition by azapeptides. Appendix: thermodynamic interpretation of the activation by concentrated salts. (2001) (41)
The ligand- and microtubule assembly-induced GTPase activity of purified calf brain tubulin. (1981) (40)
THE MOLECULAR WEIGHT OF β-LACTOGLOBULIN (1957) (39)
The interaction of vincristine with calf brain tubulin. (1980) (39)
Interaction of vinblastine with calf brain tubulin: effects of magnesium ions. (1986) (38)
Mechanism of colchicine binding to tubulin. Tolerance of substituents in ring C' of biphenyl analogues. (1991) (38)
Effect of colchicine analogues on the dissociation of alpha beta tubulin into subunits: the locus of colchicine binding. (1994) (37)
NEAR INFRARED INVESTIGATION OF INTERAMIDE HYDROGEN BONDING IN AQUEOUS SOLUTION. (1964) (37)
Aging of tubulin at neutral pH. (1982) (37)
Association of αs-casein C in the alkaline pH range (1968) (35)
THE SOLUTION PROPERTIES OF BETA-LACTOGLOBULIN C. (1964) (33)
[10] Light scattering and differential refractometry (1973) (33)
The use of small-angle x-ray scattering to determine protein conformation. (1971) (33)
Molecular Interactions in β-Lactoglobulin. VII. The “Hybridization” of β-Lactoglobulins A and B2 (1961) (33)
Physical and spectroscopic methods for the evaluation of the interactions of antimitotic agents with tubulin. (1991) (33)
Molecular interactions in β-lactoglo-bulin. I. The electrophoretic heterogeneity of β-lactoglobulin close to its isoelectric point. (1960) (32)
Cooperative multiple binding of bisANS and daunomycin to tubulin. (1994) (29)
[38]Physical properties of purified calf brain tubulin (1982) (29)
The calculation of partial specific volumes of proteins in 8 M urea solution. (1981) (28)
Linkage between ligand binding and control of tubulin conformation. (1992) (28)
Heat capacity microcalorimetry of the in vitro reconstitution of calf brain microtubules. (1979) (27)
Investigation of the carboxyl ionization of β-lactoglobulin by differential infrared spectroscopy (1959) (27)
2 – Optical Spectroscopy of Proteins (1982) (27)
8 Some Physical Probes of Enzyme Structure in Solution (1970) (27)
Linkages in tubulin-colchicine functions: the role of the ring C (C') oxygens and ring B in the controls. (1998) (26)
Enzyme structure. Part L. (1986) (26)
Vincristine-induced self-association of calf brain tubulin. (1985) (25)
The pH dependence of the association of β-lactoglobulin (1956) (25)
The partial purification and some physical properties of cathepsin C from beef spleen. (1959) (25)
Studies on acid deoxyribonuclease. VII. Conformation of three nucleases in solution. (1970) (24)
β-Lactoglobulin variation in milk from individual cows (1965) (24)
THE ASSOCIATION BEHAVIOR OF β-LACTOGLOBULINS A AND B (1958) (23)
The Interactions of Proteins with Salts, Amino Acids, and Sugars at High Concentration (1991) (22)
Roles of ring C oxygens in the binding of colchicine to tubulin. (1991) (22)
Linkages between the dissociation of alpha beta tubulin into subunits and ligand binding: the ground state of tubulin is the GDP conformation. (1994) (22)
Infrared titration of lysozyme carboxyls. (1972) (22)
The molecular weight of ribonucleic acid prepared from ascites-tumor cells. (1958) (22)
Structural and Genetic Implications of the Physical and Chemical Differences Between β-Lactoglobulins A and B (1962) (22)
On the mechanism of ?-chymotrypsin dimerization (1969) (21)
Calculation of partial specific volumes of proteins in 8 M urea solution. (1981) (20)
Velocity sedimentation study of ligand-induced protein self-association. (1985) (19)
Small-angle x-ray scattering. (1973) (19)
Conformational Transitions of Bovine P-Lactoglobulins A, B, and C (1966) (18)
STUDIES OF MOLECULAR INTERACTION IN ISOIONIC PROTEIN SOLUTIONS BY LIGHT-SCATTERING. (1955) (18)
Stoichiometric and substoichiometric inhibition of tubulin self-assembly by colchicine analogues. (1996) (18)
The circular dichroism of phosvitin. (1967) (18)
Measurement and analysis of ligand-binding isotherms linked to protein self-associations. (1985) (18)
Abnormal solubility behavior of beta-lactoglobulin: salting-in by glycine and NaCl. (1987) (17)
Energy transfer studies of the distances between the colchicine, ruthenium red, and bisANS binding sites on calf brain tubulin. (1994) (17)
Structure of a magnesium-induced polymer of calf brain microtubule protein. (1974) (16)
Inhibition of tubulin self-assembly and tubulin-colchicine GTPase activity by guanosine 5'-(gamma-fluorotriphosphate). (1987) (16)
Low pH dimerization of chymotrypsin in solution. (1978) (16)
Calculation of the partial specific volume of proteins in concentrated salt and amino acid solutions. (1985) (16)
Light Scattering Investigation of Ordering Effects in Silicotungstic Acid Solutions (1959) (16)
The Fractionation of Insulin by Electrophoresis—Convection1 (1953) (15)
Diffraction methods for biological macromolecules. Part A. (1985) (15)
Optical activity of insulin. I. On the nature of the circular dichroism bands. (1971) (14)
Colchicine analogues that bind reversibly to tubulin define microtubular requirements for newly synthesized protein secretion in rat lacrimal gland. (1989) (14)
Chromatography of Ehrlich ascites tumor cell high molecular weight ribonucleic acid on calcium phosphate. (1961) (13)
The colchicine-induced GTPase activity of tubulin: state of the product. Activation by microtubule-promoting cosolvents. (1994) (13)
The effect of ionization on the light scattering of isoionic proteins. (1956) (13)
Small-Angle X-Ray Scattering Measurements of Biopolymer Molecular Weights in Interacting Systems (1973) (13)
On the electrophoretic heterogeneity of trypsin. (1956) (12)
The in vitro assembly of microtubules from purified brain tubulin (1979) (12)
Electrophoresis—Convection Applied to the Complexed Insulin—Protamine System1 (1953) (12)
Preparation and characterization of des-C-terminal tubulin (1989) (12)
Light scattering and differential refractometry. (1973) (12)
Specific interactions in proteins due to proton fluctuations (1966) (12)
Energy-transfer studies of the distance between the high-affinity metal binding site and the colchicine and 8-anilino-1-naphthalenesulfonic acid binding sites on calf brain tubulin. (1988) (12)
Light scattering of isoionic conalbumin. (1957) (12)
Molecular weight of beef heart lactate dehydrogenase. (1972) (12)
The role of tyrosines in elastase. (1972) (11)
On light-scattering studies of isoionic proteins. (1960) (11)
Cosolvent modulation of the tubulin-colchicine GTPase-activating conformational change: strength of the enzymatic activity. (1994) (11)
Investigations on proteins and polymers. V. Interaction of egg albumin with dodecylamine hydrochloride. (1951) (11)
Enzyme structure. I: Physical methods. 1: Unfolding and refolding of proteins (1986) (11)
Light and small angle X-ray scattering and biological macromolecules (1964) (11)
The interactions of tropolone with magnesium ions and tubulin. (1982) (11)
Light-scattering studies on ascites tumor cell RNA. (1960) (11)
Aging of tubulin at neutral pH: the destabilizing effect of vinca alkaloids. (1992) (11)
On The Aggregation Of Boving Serum Albumin In Acid pH (1956) (11)
In vitro formation of filaments from calf brain microtubule protein. (1975) (10)
Cotton effects in the β-lactoglobulins (1965) (9)
Preferential Interactions of Proteins with (9)
THE DISTRIBUTION OF POLIO ANTIBODIES IN SERUM PROTEINS. (1956) (8)
The state of plasma albumin in acid pH. (1957) (8)
Chemical and physico-chemical characterization of genetic variant D of bovine beta-lactoglobulin. (1969) (8)
β-Lactoglobulin As A Model of Subunit Enzymes† (1969) (7)
The circular dichroism of the beta structure of poly-L-lysine. (1966) (7)
12 – Light Scattering1 (1970) (7)
Aging of tubulin at neutral pH: stabilization by colchicine and its analogues. (1992) (7)
Criteria for distinguishing self-associations in velocity sedimentation. (1986) (7)
Enthalpy changes in microtubule assembly from pure tubulin. (1986) (7)
[Mechanism of stabilization of proteins by glycerol and sucrose]. (1982) (7)
Aggregation Phenomena in Polyvinyl Alcohol-Acetate Solutions. (1949) (6)
Semicontinuous electrophoresis-convection. (1953) (6)
The resolution of bimodal peaks in the analytical ultracentrifuge in the presence and absence of ligands. (1983) (6)
Fractionation of ragweed extract by semicontinuous electrophoresis-convection. (1955) (6)
Investigations on proteins and polymers. VI. Interaction of egg albumin with a thiophene-2-azlactone. (1951) (6)
Difference infrared spectrophotometric titration of protein carboxyls. (1973) (6)
Interaction of vincristine with calf brain tubulin. (1983) (6)
Structural analysis of the substoichiometric and stoichiometric microtuble-inhibiting biphenyl analogues of colchicine. (1996) (6)
Physical properties of purified calf brain tubulin. (1982) (6)
A light‐scattering cell for angular measurements (1959) (6)
Optical activity of insulin. II. Effect of nonaqueous solvents. (1971) (6)
A solution physical-chemical examination of the self-association of tubulin. (1976) (5)
The enzymic activity of trypsin autolysis products. (1966) (5)
Polymerization and Calcium Binding of the Tubulin-colchicine Complex in the GDP State (2003) (5)
Quasielastic light scattering studies of tubulin aggregation. (1987) (5)
Experimental Investigation of Fractionation in the Electrophoresis—Convection Apparatus (1952) (5)
Aminolysis and Alcoholysis of a Thiophene Azlactone (1951) (4)
Investigations on proteins and polymers. IX. Denaturation studies of egg albumin with aliphatic amines. (1952) (4)
Light-Scattering Study of the Interaction of β-Lactoglobulin Solvent Components in the System Water-2-Chloroethanol (1968) (4)
A New Absolute-Scale Small-Angle X-Ray Scattering Instrument (1969) (4)
Infrared investigation of the secondary structure of beta-lactoglobulins. (1966) (4)
The Application of Light Scattering and Small-Angle X-Ray Scattering to Interacting Biological Systems (1963) (3)
Stabilization And Destabilization By Co-Solvents (2002) (3)
Role of the dianionic form of the GTP gamma-phosphate in the polymerization process of tubulin. (1985) (3)
THE MACROMOLECULAR PARAMETERS OF ASCITES TUMOR CELL H-RNA. (1964) (3)
Association properties of trypsin inhibitors from lima bean. (1973) (3)
Enzyme structure. J.I.: Size, shape, and polydispersity of macromolecules (1985) (3)
On the inhibition of chymotrypsin by ovomucoid. (1960) (3)
Modification of lima bean proteinase inhibitor with catalytic amounts of bovine and porcine trypsins (1974) (3)
Communication to the Editor: The Quadratic Term in the Light-Scattering Equation. (1949) (3)
Electrophoresis-convection Applied to Substances Forming Soluble Complexes1 (1952) (3)
Concerning trans-Acylation in Azlactone Synthesis (1951) (2)
Symposium on Structure of Enzymes and Proteins: Sponsored by the Biology Division, Oak Ridge National Laboratory, Gatlinburg, Tennessee, April 4–6, 1955. Reprinted from the Journal of Cellular and Comparative Physiology 47, Supplement 1, May 1956. 294 pp (1957) (2)
Enzyme structure. I: Physical methods. 2: Structural dynamics and mobility of proteins (1986) (2)
Ultracentrifugal Behaviors of the Tubulin-Colchicine Complex in the State of GTP in Different Buffers (2003) (1)
The state of amino acid residues in beta-lactoglobulin. (1969) (1)
On the mechanism of alpha-chymotrypsin dimerization. (1969) (1)
The role of double rings in the tubulin‐microtubule cycle: Linkage with nucleotide binding (2008) (1)
THE BIOPHYSICAL APPROACH TO THE SELF-ASSEMBLY OF BIOLOGICAL ORGANELLES: THE TUBULIN - MICROTUBULE SYSTEM1 (1981) (1)
Preferential Binding of Solvent Components to Protein In Mixed Water–Organic Solvent Systems† (1969) (1)
The tribulations of a stateless European child in his discovery of America and his thorny path to protein thermodynamics (2004) (1)
MECHANISMS OF PROTEIN STABILIZATION AND DESTABILIZATION BY SOLVENT COMPONENTS (1976) (1)
Erratum: The reconstitution of microtubules from purified calf brain tubulin (Biochemistry (1975) 14, 23, (5183-5187)) (1976) (1)
Vapor Phase Crystallization (2002) (1)
Reversible interaction of purified tubulin with colchicine analogues (1984) (1)
[On protein-structure stabilizing solvent]. (1982) (1)
Association of alpha-S-casein C in the alkaline pH range. (1968) (1)
Mechanism of the inhibition of protein secretion by colchicine (1988) (1)
Abstract of papers presented at the Twenty-Sixth Annual Meeting of the Society for Cryobiology June 11–16, 1989, Charleston, South Carolina Symposium I—Cryosensitizing and cryoprotective agentsMechanism of stabilization of protein structure by solvents and co-solvents☆☆☆ (1989) (1)
Cotton effects in the beta-lactoglobulins. (1965) (0)
Linked Functions: Binding and Linkage . Functional Chemistry of Biological Macromolecules. Jeffries Wyman and Stanley J. Gill. University Science, Mill Valley, CA, 1990. xvi, 330 pp., illus. $44.50. (1991) (0)
Enzyme structure. J. II: Interaction of macromolecules with ligands and linkages (1985) (0)
Enzyme structure. K.2: Macromolecular conformation: spectroscopy (1986) (0)
Transfer Free Energy (2002) (0)
Enzyme structure. K.3: Macromolecular conformational stability and transitions (1986) (0)
Problem-driven biochemistry (1976) (0)
Calcium binding to the tubulin-colchicine complex in the state of GTP in a BBS buffer (2002) (0)
Investigation of the carboxy ionization of beta-lactoglobulin by differential infrared spectroscopy. (1959) (0)
The optical rotatory dispersion of the beta-lactoglobulins. (1966) (0)
Principles and problems in physical chemistry for biochemists: by Nicholas C. Price and Raymond Dwek, published by Clarendon Press, Oxford. Hard back £5.50; paperback £2.35 (186 pages) (1976) (0)
Linked functions. (1991) (0)
ST056390 Colchicine (2018) (0)
The geometry of the β-lactoglobulins in various states of aggregation. (1962) (0)
Mechanism of the modulation of biological reactions by cosolvents (2000) (0)
The binding of vinca alkaloids to calf brain tubulin (1975) (0)
Enzyme Structure. Vol. 49, Pt. G (1978) (0)
Errata: Reconstitution of microtubules from purified calf brain tubulin (Biochemistry (1975) 14(23) (5183–5187) (10.1021/bi00694a025)) (1976) (0)
CRYSTALLIZE FROM 2-METHYL-2 , 4-PENTANEDIOL ? (2019) (0)
John G. Kirkwood, 1907-1959. (1960) (0)
Enzyme structure. K.1: Macromolecular self-associations and structural assemblies (1986) (0)
The pH dependence of the association of beta-lactoglobulin. (1956) (0)
A magnesium induced formation of filaments from purified calf brain tubulin (1975) (0)
Salting In, Salting Out (2002) (0)
Biological macromolecules and polyelectrolytes in solution: By Henryk Eisenberg, Oxford University Press (Clarendon), London, 1976. xvii + 272 pp. £16.00 (1978) (0)
Equilibrium behavior of the β-lactoglobuh'ns in the A-B tetramer. (1963) (0)

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Fordham University