Oleg B. Ptitsyn

Oleg B. Ptitsyn's AcademicInfluence.com Rankings

Oleg B. Ptitsyn

Mathematics

#6468

World Rank

#8947

Historical Rank

Measure Theory

#1366

World Rank

#1716

Historical Rank

mathematics Degrees

Oleg B. Ptitsyn

Biology

#9310

World Rank

#12499

Historical Rank

Molecular Biology

#1260

World Rank

#1287

Historical Rank

biology Degrees

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Mathematics
Biology

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Oleg B. Ptitsyn's Published Works

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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

Molten globule and protein folding. (1995) (1132)
Evidence for a molten globule state as a general intermediate in protein folding (1990) (607)
α‐lactalbumin: compact state with fluctuating tertiary structure? (1981) (537)
Protein folding: Hypotheses and experiments (1987) (481)
Conserved residues and the mechanism of protein folding (1996) (298)
The ‘molten globule’ state is involved in the translocation of proteins across membranes? (1988) (258)
Why do globular proteins fit the limited set of folding patterns? (1987) (253)
Theory of protein secondary structure and algorithm of its prediction (1983) (214)
"Domain" Coil-Globule Transition in Homopolymers (1995) (209)
Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface. (1996) (202)
Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. (1996) (198)
A model of myoglobin self-organization. (1975) (193)
Structures of folding intermediates. (1995) (193)
Similarities of protein topologies: evolutionary divergence, functional convergence or principles of folding? (1980) (179)
"Partly folded" state, a new equilibrium state of protein molecules: four-state guanidinium chloride-induced unfolding of beta-lactamase at low temperature. (1994) (175)
Sequential mechanism of refolding of carbonic anhydrase B (1987) (174)
‘Molten‐globule“ state accumulates in carbonic anhydrase folding (1984) (159)
The molten globule is a third thermodynamical state of protein molecules (1994) (158)
Comparison of predicted and experimentally determined secondary structure of adenyl kinase (1974) (151)
Cooperativity of the Coil-Globule Transition in a Homopolymer: Microcalorimetric Study of Poly(N-isopropylacrylamide) (1994) (150)
Conformations of Macromolecules (1966) (134)
Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes? (1998) (124)
Retinol-binding protein is in the molten globule state at low pH. (1992) (123)
[Stages in the mechanism of self-organization of protein molecules]. (1973) (116)
How the molten globule became. (1995) (113)
Non-functional conserved residues in globins and their possible role as a folding nucleus. (1999) (107)
Kinetic and equilibrium folding intermediates. (1995) (104)
Empirical solvent‐mediated potentials hold for both intra‐molecular and inter‐molecular inter‐residue interactions (1998) (96)
Statistical analysis of the distribution of amino acid residues among helical and non-helical regions in globular proteins. (1969) (92)
Kinetic and equilibrium intermediates in protein folding. (1994) (91)
An early immunoreactive folding intermediate of the tryptophan synthase β2 subunit is a ‘molten globule’ (1990) (90)
How does protein synthesis give rise to the 3D‐structure? (1991) (88)
Compact state of a protein molecule with pronounced small-scale mobility: bovine α-lactalbumin (2004) (82)
‘All‐or‐none’ mechanism of the molten globule unfolding (1992) (80)
Alpha-Lactalbumin: compact state with fluctuating tertiary structure? (1981) (78)
Statistical analysis of the correlation among amino acid residues in helical, beta-structural and non-regular regions of globular proteins. (1971) (77)
Physical reasons for secondary structure stability: α‐Helices in short peptides (1991) (72)
All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins. (1996) (69)
A theory of protein molecule self-organization. IV. Helical and irregular local structures of unfolded protein chains. (1976) (68)
The models of the denaturation of globular proteins. I. Theory of globula–coil transitions in macromolecules (1967) (67)
How molten is the molten globule? (1996) (66)
Folding intermediates are involved in genetic diseases? (1995) (64)
Quasielastic light scattering from human α-lactalbumin: comparison of molecular dimensions in native and ‘molten globule’ states (1986) (63)
Protein structure and neutral theory of evolution. (1986) (56)
Thermodynamic parameters of helix‐coil transition in polypeptide chains I. Poly‐(L‐glutamic acid) (1971) (54)
De novo design, synthesis and study of albebetin, a polypeptide with a predetermined three-dimensional structure. Probing the structure at the nanogram level. (1992) (53)
Thermodynamic parameters of helix–coil transition in polypeptide chains. II. Poly‐L‐lysine (1971) (52)
The models of the denaturation of globular proteins. II. Hydrophobic interactions and conformational transition in polymethacrylic acid (1967) (51)
Theory of protein molecule self‐organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments (1977) (44)
Correlation between enzyme activity and hinge-bending domain displacement in 3-phosphoglycerate kinase. (1989) (40)
Comparison of intramolecular packing of a protein in native and ‘molten globule’ states (1986) (39)
Thermodynamic parameters of helix-coil transitions in polypeptide chains (1972) (39)
Principal folding pathway and topology of all‐β proteins (1979) (36)
Theory of protein molecule self‐organization. I. Thermodynamic parameters of local secondary structures in the unfolded protein chain (1977) (34)
Nanosecond dynamics of tryptophans in different conformational states of apomyoglobin proteins. (2000) (34)
Release of retinol and denaturation of its plasma carrier, retinol-binding protein. (1998) (34)
Binding of the globular domain of linker histones H5/H1 to the nucleosome: a hypothesis. (1989) (33)
Method of determining the relative stability of different conformational states of biological macromolecules (1969) (32)
Invariant features of globin primary structure and coding of their secondary structure (1974) (29)
Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin. (1985) (26)
Noncooperative temperature melting of a globular protein without specific tertiary structure: Acid form of bovine carbonic anhydrase B (1985) (25)
Inter‐domain mobility in proteins and its probable functional role (1978) (24)
X-ray diffuse scattering by proteins in solution. Consideration of solvent influence (1974) (23)
A determinable but unresolved problem (1996) (22)
Potentiometric titration of polyacrylic acid, polymethacrylic acid and poly-l-glutamic acid (1965) (22)
X‐Ray diffuse scattering of globular protein solutions: Consideration of the solvent influence (1972) (22)
Secondary structure formation and stabilityCurrent Opinion in Structural Biology 1992, 2:1320 (1992) (22)
Direct energy transfer to study the 3D structure of non-native proteins: AGH complex in molten globule state of apomyoglobin. (1999) (21)
Molten globule versus variety of intermediates: influence of anions on pH‐denatured apomyoglobin (1999) (21)
Mechanism of pH‐induced release of retinol from retinol‐binding protein (1993) (20)
Prediction of protein secondary structure based on physical theory. Histones. (1989) (20)
Physical reasons for secondary structure stability: alpha-helices in short peptides. (1991) (18)
The structure of ribonuclease in solution does not differ from its crystalline structure (1978) (17)
[Determination of the secondary structure of proteins from their circular dichroism spectra. I. Protein reference spectra for alpha-, beta- and irregular structures]. (1980) (17)
Identification of the secondary structure of polypeptide chains in solution by x‐ray diffusion scattering (1971) (16)
Polarized luminescence and mobility of tryptophan residues in polypeptide chains (1981) (16)
Mechanism of protein folding (1979) (16)
On the presence of a dense internal region in the 50 S subparticle of E. coli ribosomes (1970) (15)
Can grafting of an octapeptide improve the structure of a de novo protein? (1998) (15)
A study of apo‐ and holo‐forms of horse liver alcohol dehydrogenase in solution by diffuse X‐ray scattering (1986) (15)
Determination of the thermodynamic characteristics of the conformational transition in polymethacrylic acid from potentiometric titration curves (1968) (15)
Short alpha-helix stability (1990) (14)
[Protein globule without the unique three-dimensional structure: experimental data for alpha-lactalbumins and general model]. (1982) (13)
Random sequences and protein folding (1985) (12)
Protein folding: nucleation and compact intermediates. (1998) (12)
The geometry of linear polymers—VIII. An approximate statistical theory of volume effects in linear polymer chains (1962) (11)
[Fluctuating state of the protein globule]. (1983) (11)
Hydrophobic interaction and conformational transitions in polymethacrylic acid (1965) (11)
Folding and binding. From theory to therapy. (1997) (11)
[Determination of protein secondary structure from circular dichroism spectra. III. Protein-derived base spectra of circular dichroism for antiparallel and parallel beta-structures]. (1981) (10)
Dipole–dipole interaction and the β structure of synthetic polypeptides (1967) (10)
Thermodynamic parameters of the helix–coil transition in polypeptide chains. III. Random copolymers of L‐leucine with L‐glutamic acid (1975) (9)
Viscometric study of conformational transition in ionization of polymethacrylic acid (1968) (9)
An early intermediate of refolding alpha-lactalbumin forms within 20 ms. (1987) (9)
Microtacticity of polymers and methods of its investigation (1961) (9)
Calculation of volume effects in macromolecules by means of a Monte Carlo method: Non-self-intersecting chains on a cubic lattice☆ (1967) (8)
Intramolecular interactions in polymer chains (1960) (8)
[Preparation and study of albebetin, an artificial protein with a given spatial structure]. (1991) (7)
Secondary-structure formation and stability (1992) (6)
[Relation of the secondary structure of globular proteins to their primary structure]. (1970) (6)
A new approach to artificial and modified proteins: theory-based design, synthesis in a cell-free system and fast testing of structural properties by radiolabels. (1994) (5)
Physical principles of protein structure and protein folding (1985) (5)
Protein Evolution and Protein Folding: Non-Functional Conserved Residues and Their Probable Role (1998) (5)
Folding and binding: The biological consequences of physical principles (1999) (5)
[Structure of lysozyme and its complex with an inhibitor in solution: comparison with crystalline structures]. (1976) (4)
The interpretation of experimental data on the translational friction of flexible macromolecules in good solvent (1962) (4)
[Determination of the secondary structure of proteins from their circular dichroism spectra. II. Estimation of the contribution of beta-pleated sheets]. (1980) (3)
Hydrodynamics of polymer solutions—III. Influence of volume effects on light scattering and the friction coefficient of macromolecules in solution☆ (1960) (3)
[Folding and topology of antiparallel beta-structure]. (1979) (3)
[The state of unfolded globules of protein molecules is more quickly becoming a rule, rather than an exception]. (1993) (3)
[Molten globule unfolding by strong denaturing agents occurs by the "all or nothing" principle]. (1993) (3)
[THE THEORY OF HELIX-COIL TRANSITIONS IN MACROMOLECULES]. (1965) (3)
PROTEIN ENGINEERING OF MAN-MADE PROTEINS: A REVIEW (1996) (3)
[Intramolecular mobility of a protein in a "molten globule" state. A study of carbonic anhydrase by 1H-NMR]. (1989) (3)
Dimensions of branched macromolecules in good solvents (1963) (3)
Quasirandom distribution of α and β regions in globular proteins (1983) (2)
Prediction of the three‐dimensional structure for ribosomal protein L25 (1975) (2)
The structure and flexibility of stereoregular macromolecules. The model of statistical zigzag chain (1967) (2)
The models of the denaturation of globular proteins. III. The intramolecular β-structure coil transitions in poly-S-carbobenzoxymethyl-l-cysteine (1967) (2)
Principal folding pathway and topology of all-beta proteins. (1979) (2)
Theory of polyelectrolyte solutions—V. Short-range interaction of charged groups in stereoregular polyelectrolytes (1964) (2)
The structure of hydrophobic cores of globins. (1975) (2)
Geometry of linear polymers—VI. The theory of volume effects in polymer chains (1960) (1)
[Protein as an edited random copolymer]. (1984) (1)
[X-ray diffuse scattering by polypeptides and proteins in solution. IV. Consideration of the solvent effect for globular protein solutions]. (1974) (1)
The Monte Carlo method of calculating volume effects in linear polymer chains (1964) (1)
[Self-organization of the myoglobin molecule]. (1973) (1)
Internal rotation in polymer chains and their physical properties—XIX. Rotational isomerization of polymer molecules on stretching and methods for its investigation (1964) (1)
[Predicting the spiral portions of globular proteins from their primary structure]. (1970) (1)
[De novo proteins with a given spatial structure: new approaches to design and analysis]. (1992) (1)
THE TRANSITION INTO THE VITREOUS STATE AND THE HYDROGEN BONDS (1959) (1)
Molecular interactions in polymer solutions— I. The influence of volume effects on the second virial coefficient (1960) (1)
MECHANISM OF SELF-ORGANIZATION OF THE TERTIARY STRUCTURE OF GLOBULAR PROTEINS (1981) (1)
[On the kinetics of biosynthesis]. (1963) (1)
Hydrodynamics of polymer solutions—VI. Intrinsic viscosity of partially penetrable flexible macromolecules in good solvents☆☆☆ (1964) (1)
[Effect of a biologically active interferon fragment on the structure of the synthetic protein carrier]. (1998) (1)
Interdomain mobility of enzymes and its functional role (1988) (1)
Dimensions of graft polymers (1966) (1)
[Compact structure of random copolymers of hydrophobic and hydrophilic amino acid residues]. (1980) (1)
[Protein engineering of artificial proteins]. (1996) (1)
DE NOVO PROTEIN WITH A PREDETERMINED THREE-DIMENSIONAL STRUCTURE : NEW APPROACHES TO CONSTRUCTION AND ANALYSIS (1992) (0)
Thermodynamic parameters of helix-random coil transitions in polypeptide chains. IV. Random copolymers of L-alanine with L-glutamic acid. (1976) (0)
[Kinetics of the renaturation of bovine alpha-lactalbumin]. (1988) (0)
An early immun~r~a~tiv~ folding intermediate of the trypt~phan synthase /I2 subunit is a 'molten globuk' (1990) (0)
Dipole-dipole interaction and the beta structure of synthetic polypeptides. (1967) (0)
[Effect of electrostatic interactions on the dimensions of native DNA molecules]. (1967) (0)
Mikhail Vladimirovich Vol'kenshteĩn (on his 70th birthday) (1982) (0)
Investigations of synthetic polypeptides: transitions-intramolecular beta-structures-coil in poly-S-carbobenzoxymethyl-L-cysteine. (1966) (0)
[The functional state of denatured proteins: the principles of modelling and the first results]. (1995) (0)
[Letter: Helical structure of unfolded protein chains]. (1974) (0)
[Self-organization of protein structures--a bridge between physics and biology]. (1999) (0)
Protein Engineering of Albebetin, A de Novo Protein with a Predesigned Three-Dimensional Structure (1996) (0)
[Hydrophobic interactions and nucleoprotein structure]. (1966) (0)
[Studies of synethtic polypeptides. II. Beta-structure--coil transition of poly-S-carboxymethyl-L-cysteine under changes of medium pH and temperature]. (1966) (0)
Contents to volume 224 (2001) (0)
[Three-stage equilibrium unfolding of small globular proteins by denaturing agents. I. Carboanhydrase B]. (1996) (0)
Stereospecific influence of the end of the growing chain on the polymerization of charged monomers (1964) (0)
THREE-STAGE EQUILIBRIUM UNFOLDING OF SMALL GLOBULAR PROTEINS BY STRONG DENATURANTS. II. BETA -LACTAMASE AND GENERAL MODEL (1996) (0)
A New Approach to Artificial Proteins: Theory-Based Design. Synthesis in the Cell-Free System and Structural Probing at the Nanogram Level (1993) (0)
[Theory of self-organization of the secondary structure of proteins: relationship between native globule structure and the secondary structure of the unfolded chain]. (1978) (0)
The hydrodynamics of polymer solutions—VII. The effect of long range interaction on the intrinsic viscosity of linear macromolecules near the θ-point (1964) (0)
[The physical principles of the self-organization of protein bonds]. (1970) (0)
Diffuse scattering of x-rays by solutions of synthetic polypeptides and globular proteins. (1974) (0)
[The theory of spiral-coil transition in biopolymers. II. The role of distant order interaction in DNA denaturation]. (1962) (0)
[Theory of helix-coil transformation in biopolymers. V. A method of determining cooperativeness of helix-coil transformation in polypeptide chains by changing molecule size in the transformation region]. (1965) (0)
Stereospecificity of polymers as a function of the conditions of polymerization (1960) (0)
[Y97V substitution in the horse cytochrome c causes accumulation of the equilibrium intermediate]. (2001) (0)
[Multicenter mechanism of self-organization of globular proteins and cooperativity of their denaturation and renaturation]. (1975) (0)
[ON A STUDY OF THE STRUCTURE OF MOLECULES OF NATIVE RNA BY THE METHOD OF SCATTERING ROENTGEN RAYS AT SMALL ANGLES]. (1963) (0)
[Study of synthetic polypeptides. I. Transformations-intramolecular beta-structure coil in poly-S-carbobenzoxymethyl-L-cysteine]. (1965) (0)
[Predicting the three-dimensional structure of alpha- and beta-interferons]. (1986) (0)
Mikhail Vladimirovich Vol'kenshtein (on his 70th birthday) (1982) (0)
[DETERMINATION OF FLEXIBILITY OF DNA MOLECULES WITH THE AID OF LIGHT DISSEMINATED AT LARGE ANGLES]. (1963) (0)
THE STRUCTURE OF A DE NOVO CARRIER PROTEIN AS AFFECTED BY A GRAFTED INTERFERON FRAGMENT POSSESSING BIOLOGICAL ACTIVITY (1998) (0)
Statistical theory of volume effects in macromolecules (1963) (0)
Method of determining the relative stability of different conformational states of biopolymer molecules (1970) (0)
[Three-stage equilibrium unfolding of small globular proteins by denaturing agents. II. Beta-lactamase and general model]. (1996) (0)
THREE-STAGE EQUILIBRIUM UNFOLDING OF SMALL GLOBULAR PROTEINS BY STRONG DENATURANTS. I. CARBONIC ANHYDRASE B (1996) (0)
[Lattice model of portions of the protein molecule hydrophobic nucleus]. (1972) (0)
[Synthetic polypeptides. 3. Comparison of the degree of cooperation of the helical state of poly-L-glutaminic acid in various solvents]. (1967) (0)
[Folding and topology of parallel beta-structure]. (1979) (0)
[The nature of forces determining the inherent spatial structure of globular proteins]. (1967) (0)
[Synthesis of poly-S-carbobenzomethoxy-L-cysteine and studies on its structure]. (1965) (0)
[Identification of alpha-spiral structure of polypeptide chains in solution by x-ray diffusion scattering]. (1971) (0)
[Nature of the 4.5 Angstrom-maximum in x-ray diffraction curves of proteins and structured polypeptides]. (1977) (0)
Physical principles of protein structures (1983) (0)

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