Kunihiro Kuwajima
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Kunihiro Kuwajima's Degrees
- PhD Computer Science University of Tokyo
- Masters Computer Science University of Tokyo
- Bachelors Computer Science University of Tokyo
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(Suggest an Edit or Addition)Kunihiro Kuwajima'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
- The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure (1989) (1251)
- Role of the molten globule state in protein folding. (2000) (420)
- The molten globule state of α‐lactalbumin (1996) (380)
- Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin. (1985) (271)
- Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of alpha-lactalbumin and lysozyme. (1986) (248)
- α-Lactalbumin: A calcium metalloprotein (1980) (232)
- Three-state denaturation of α-lactalbumin by guanidine hydrochloride (1976) (222)
- Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism (1987) (212)
- Folding of green fluorescent protein and the cycle3 mutant. (2000) (182)
- A folding model of α-lactalbumin deduced from the three-state denaturation mechanism (1977) (155)
- Protein globularization during folding. A study by synchrotron small-angle X-ray scattering. (1996) (154)
- Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics of alpha-lactalbumin. (1989) (145)
- Rapid formation of a molten globule intermediate in refolding of α-lactalbumin (1996) (143)
- Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. (1991) (136)
- Structural characterization of the molten globule of α‐lactalbumin by solution X‐ray scattering (1997) (135)
- Acid denaturation and refolding of green fluorescent protein. (2004) (126)
- Kinetics of disulfide bond reduction in alpha-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond. (1990) (117)
- The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. (1996) (108)
- Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra. (1991) (102)
- Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy. (1998) (98)
- Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry. (1992) (92)
- Detection and characterization of the intermediate on the folding pathway of human alpha-lactalbumin. (1978) (92)
- Mutational analysis of protein solubility enhancement using short peptide tags. (2007) (91)
- An early immunoreactive folding intermediate of the tryptophan synthase β2 subunit is a ‘molten globule’ (1990) (90)
- Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli. (1999) (90)
- Fast Compaction of α-Lactalbumin During Folding Studied by Stopped-flow X-ray Scattering (2002) (89)
- The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state (1994) (88)
- Unification of the folding mechanisms of non-two-state and two-state proteins. (2004) (78)
- Ca2+-induced alteration in the unfolding behavior of alpha-lactalbumin. (1986) (76)
- Is folding of β-lactoglobulin non-hierarchic? intermediate with native-like β-sheet and non-native α-helix (2000) (76)
- Influence of Ca2+ binding on the structure and stability of bovine alpha-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra. (2009) (70)
- Folding-unfolding equilibrium and kinetics of equine beta-lactoglobulin: equivalence between the equilibrium molten globule state and a burst-phase folding intermediate. (1999) (60)
- Protein folding in vitro. (1992) (58)
- Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy. (1998) (55)
- Folding of carp parvalbumin studied by equilibrium and kinetic circular dichroism spectra (1988) (51)
- Effects of amino acid substitutions in the hydrophobic core of alpha-lactalbumin on the stability of the molten globule state. (1995) (50)
- Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP. (2001) (50)
- Secondary structure of globular proteins at the early and the final stages in protein folding (1993) (49)
- Equilibrium and kinetics of the thermal unfolding of alpha-lactalbumin. The relation to its folding mechanism. (1978) (49)
- Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme. (2000) (47)
- Role of the Helical Protrusion in the Conformational Change and Molecular Chaperone Activity of the Archaeal Group II Chaperonin* (2004) (47)
- Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride (II) (1976) (45)
- Molecular Mechanisms of the Cytotoxicity of Human α-Lactalbumin Made Lethal to Tumor Cells (HAMLET) and Other Protein-Oleic Acid Complexes* (2013) (45)
- Effect of GroEL on the Re-folding Kinetics of α-Lactalbumin (1996) (45)
- Exchange behavior of the H-bonded amide protons in the 3 to 13 helix of ribonuclease S. (1983) (44)
- Contribution of the 6-120 disulfide bond of alpha-lactalbumin to the stabilities of its native and molten globule states. (1992) (44)
- Multiple parallel-pathway folding of proline-free Staphylococcal nuclease. (2003) (43)
- Innocuous character of [ethylenebis(oxyethylenenitrilo)]tetraacetic acid and EDTA as metal-ion buffers in studying Ca2+ binding by alpha-lactalbumin. (1986) (41)
- Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding. (2000) (41)
- Effects of proline mutations on the folding of staphylococcal nuclease. (1999) (41)
- The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein. (2006) (41)
- Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human α-lactalbumin by circular dichroism spectroscopy (2000) (41)
- Dominant Forces in the Recognition of a Transient Folding Intermediate of α-Lactalbumin by GroEL (1996) (40)
- Reversible and fast association equilibria of a molecular chaperone, gp57A, of bacteriophage T4. (2003) (35)
- Characterization of Archaeal Group II Chaperonin-ADP-Metal Fluoride Complexes (2005) (34)
- The Pro117 to glycine mutation of staphylococcal nuclease simplifies the unfolding—folding kinetics (1991) (33)
- Flexible Recognition of the tRNA G18 Methylation Target Site by TrmH Methyltransferase through First Binding and Induced Fit Processes* (2010) (32)
- Surprisingly high correlation between early and late stages in non-two-state protein folding. (2006) (31)
- The Catalytic Domain of Topological Knot tRNA Methyltransferase (TrmH) Discriminates between Substrate tRNA and Nonsubstrate tRNA via an Induced-fit Process* (2013) (31)
- Solubilization and folding of a fully active recombinant Gaussia luciferase with native disulfide bonds by using a SEP-Tag. (2011) (30)
- Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry (2013) (30)
- Hydrogen exchange study of canine milk lysozyme: Stabilization mechanism of the molten globule (2000) (29)
- ATP Dependent Rotational Motion of Group II Chaperonin Observed by X-ray Single Molecule Tracking (2013) (28)
- Role of the Interaction between Ionizable Groups in the Folding of Bovine α-Lactalbumin (1981) (28)
- Transition state in the folding of α‐lactalbumin probed by the 6‐120 disulfide bond (1998) (28)
- Stopped-Flow Circular Dichroism (1996) (28)
- Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: evidence for noncooperative nucleotide binding. (1999) (28)
- Different folding pathways taken by highly homologous proteins, goat alpha-lactalbumin and canine milk lysozyme. (2010) (28)
- Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein. (1999) (28)
- Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy. (2003) (28)
- Irreversible Denaturation of Maltodextrin Glucosidase Studied by Differential Scanning Calorimetry, Circular Dichroism, and Turbidity Measurements (2014) (27)
- Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES. (1999) (27)
- Helical and expanded conformation of equine beta-lactoglobulin in the cold-denatured state. (2005) (26)
- Localized Nature of the Transition-state Structure in Goat α-Lactalbumin Folding (2004) (26)
- Oligomeric Hsp33 with Enhanced Chaperone Activity (2004) (26)
- Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase. (2003) (26)
- Sequential Action of ATP-dependent Subunit Conformational Change and Interaction between Helical Protrusions in the Closure of the Built-in Lid of Group II Chaperonins* (2008) (26)
- Kinetic folding and cis/trans prolyl isomerization of staphylococcal nuclease. A study by stopped-flow absorption, stopped-flow circular dichroism, and molecular dynamics simulations. (1997) (24)
- Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering. (2008) (24)
- Experimental studies of folding kinetics and structural dynamics of small proteins. (1984) (24)
- Solvent environments significantly affect the enzymatic function of Escherichia coli dihydrofolate reductase: comparison of wild-type protein and active-site mutant D27E. (2013) (23)
- Thermodynamic characterization of partially denatured states in the denaturation process of bovine alpha-lactalbumin by inorganic denaturants. (1977) (23)
- Absence of the thermal transition in apo-α-lactalbumin in the molten globule state (1992) (23)
- The molten globule of β(2)-microglobulin accumulated at pH 4 and its role in protein folding. (2013) (23)
- Intramolecular perturbation of tryptophans induced by the protonation of ionizable groups in goat alpha-lactalbumin. (1980) (23)
- Strategy for trapping intermediates in the folding of ribonuclease and for using 1H‐NMR to determine their structures (1983) (23)
- Electrophoretic Investigations of the Acid Conformational Change of α-Lactalbumin (1975) (22)
- Denaturation and reassembly of chaperonin GroEL studied by solution X‐ray scattering (2003) (22)
- The allosteric transition of GroEL induced by metal fluoride-ADP complexes. (2003) (21)
- Application of stopped-flow circular dichroism to the study of the unfolding of proteins. (1977) (21)
- Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin. (1996) (21)
- NMR characterization of the interaction of GroEL with amyloid β as a model ligand (2013) (20)
- Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride (IV) Dependence of the N ⇌ A transconformation on temperature (1977) (19)
- Native-state heterogeneity of β(2)-microglobulin as revealed by kinetic folding and real-time NMR experiments. (2013) (19)
- Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped‐flow circular dichroism (1995) (19)
- Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL. (1998) (19)
- alpha-Lactalbumin: a calcium metalloprotein. (1980) (19)
- Nature and locations of the most slowly exchanging peptide NH protons in residues 1 to 19 of ribonuclease S. (1983) (18)
- Binding strength of calcium ion to bovine alpha-lactalbumin. (1986) (18)
- PFDB: A standardized protein folding database with temperature correction (2019) (18)
- Three-state denaturation of alpha-lactalbumin by guanidine hydrochloride. (1976) (18)
- Fibrillogenic propensity of the GroEL apical domain: A Janus‐faced minichaperone (2012) (17)
- Fast folding of Escherichia coli cyclophilin A: a hypothesis of a unique hydrophobic core with a phenylalanine cluster. (2000) (17)
- Folding‐unfolding of goat α‐lactalbumin studied by stopped‐flow circular dichroism and molecular dynamics simulations (2001) (16)
- The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins (2020) (15)
- Equilibrium and kinetics of the folding and unfolding of canine milk lysozyme. (2007) (15)
- Water and Biomolecules (2009) (15)
- Calcium-regulated interactions of human α-lactalbumin with bee venom melittin (1991) (14)
- Characterization of kinetic folding intermediates of recombinant canine milk lysozyme by stopped-flow circular dichroism. (2005) (14)
- Is folding of beta-lactoglobulin non-hierarchic? Intermediate with native-like beta-sheet and non-native alpha-helix. (2000) (13)
- Dissection of the ATP-dependent conformational change cycle of a group II chaperonin. (2014) (13)
- The H/D-exchange kinetics of the Escherichia coli co-chaperonin GroES studied by 2D NMR and DMSO-quenched exchange methods. (2013) (13)
- Phi value analysis of an allosteric transition of GroEL based on a single-pathway model. (2004) (13)
- Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: effects of ATP and ADP on the GroEL-affected refolding of alpha-lactalbumin. (2001) (13)
- Effect of an alternative disulfide bond on the structure, stability, and folding of human lysozyme. (2000) (13)
- Application of the pH-jump method to the titration of tyrosine residues in bovine alpha-lactalbumin. (1979) (12)
- Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering. (2002) (12)
- Non‐native α‐helix formation is not necessary for folding of lipocalin: Comparison of burst‐phase folding between tear lipocalin and β‐lactoglobulin (2009) (12)
- Contribution of Thr29 to the thermodynamic stability of goat α‐lactalbumin as determined by experimental and theoretical approaches (2001) (11)
- Effect of GroEL on the re-folding kinetics of alpha-lactalbumin. (1996) (11)
- Dissecting a bimolecular process of MgATP²- binding to the chaperonin GroEL. (2011) (11)
- Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL. (1996) (10)
- Kinetic correlations between the disulfide bond reduction and the induced conformational change of proteins. (1981) (10)
- Hydrogen exchange of the tryptophan residues in bovine α‐lactalbumin studied by uv spectroscopy (1988) (10)
- Solution X-ray scattering study on the chaperonin GroEL from Escherichia coli. (1995) (9)
- Hydrogen-exchange kinetics of reduced alpha-lactalbumin bound to the chaperonin GroEL. (1997) (9)
- Probing force-induced unfolding intermediates of a single staphylococcal nuclease molecule and the effect of ligand binding. (2008) (9)
- The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state. (1994) (8)
- Atomically detailed description of the unfolding of alpha-lactalbumin by the combined use of experiments and simulations. (2005) (8)
- The use of spin desalting columns in DMSO‐quenched H/D‐exchange NMR experiments (2013) (8)
- Folding-unfolding of α-lactalbumin (1983) (8)
- Calibration method for contrast reduction problem in the X-ray image-intensi er (2001) (6)
- In reply — (1995) (6)
- Unfolding pathways of goat alpha-lactalbumin as revealed in multiple alignment of molecular dynamics trajectories. (2007) (6)
- Adaptation of a hyperthermophilic group II chaperonin to relatively moderate temperatures. (2010) (5)
- Calcium-regulated interactions of human alpha-lactalbumin with bee venom melittin. (1991) (5)
- Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human alpha-lactalbumin by circular dichroism spectroscopy. (2000) (5)
- Structure-based protein folding type classification and folding rate prediction (2015) (5)
- Circular dichroism. (1995) (5)
- Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR (2018) (5)
- Folding mechanism of canine milk lysozyme studied by circular dichroism and fluorescence spectroscopy (2003) (5)
- Determination of the structural ensemble of the molten globule state of a protein by computer simulations (2019) (5)
- A folding model of alpha-lactalbumin deduced from the three-state denaturation mechanism. (1977) (5)
- The molten globule state as an intermediate of protein folding. (1993) (5)
- ErratumErratum to “Unification of the Folding Mechanisms of Non-two-state and Two-state Proteins” [J. Mol. Biol. (2004) 339, 951–965] (2004) (4)
- Sequential four‐state folding/unfolding of goat α‐lactalbumin and its N‐terminal variants (2012) (4)
- Structural insights into the stability perturbations induced by N-terminal variation in human and goat α-lactalbumin. (2013) (4)
- The use of the time-resolved X-ray solution scattering for studies of globular proteins (2002) (3)
- An Overlapping Region between the Two Terminal Folding Units of the Outer Surface Protein A (OspA) Controls Its Folding Behavior. (2018) (3)
- Antitumor Complexes Formed by Oleic Acid and Molten Globule Intermediates of Proteins (2016) (3)
- Exploring the Folding Mechanism of Small Proteins GB1 and LB1. (2019) (3)
- Equilibrium and Kinetically Observed Molten Globule States (2008) (2)
- Experimental and Simulation Studies of the Folding/Unfolding of Goat α-Lactalbumin (2009) (2)
- DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science (2022) (1)
- Hydrogen exchange of the tryptophan residues in bovine alpha-lactalbumin studied by UV spectroscopy. (1988) (1)
- Localized nature of the transition-state structure in goat alpha-lactalbumin folding. (2004) (1)
- Equilbrium and kinetics of the unfolding of alpha-lactalbumin by guanidine hydrochloride (II). (1976) (1)
- The allosteric transition of the chaperonin groel fromescherichia coli as studied by solution X-ray scattering (2006) (1)
- Oligomeric Hsp 33 with Enhanced Chaperone Activity GEL FILTRATION , CROSS-LINKING , AND SMALL ANGLE X-RAY SCATTERING ( SAXS ) (2004) (1)
- Electrophoretic investigations of the acid conformational change of alpha-lactalbumin. (1975) (1)
- Parallel folding pathway of proline-free staphylococcal nuclease studied by the stopped-flow double-jump method (2003) (1)
- [Two views of protein folding: what is the universal view?]. (2002) (1)
- 3M1145 Effect of GroEL on refolding of staphylococcal nuclease (2002) (0)
- [Kinetic pathway of globular-protein folding]. (1990) (0)
- Acid denaturation and refolding of a mutant (Cycle3) of Green Fluorescent Protein (2002) (0)
- Faculty Opinions recommendation of Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand. (2010) (0)
- 3M1045 Folding Mechanism of Canine Milk Lysozyme Studied by Circular Dichroism and Fluorescence Spectroscopy (2002) (0)
- 1P102 Comparison of burst phase folding intermediates of tear lipocalin and β-lactoglobulin(3. Protein folding and misfolding (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) (2006) (0)
- 1P116 Exploration of the second ATP-binding site of GroEL (2005) (0)
- Unfolding of single Staphycococcal Nuclease with intermolecular force spectroscopy (2001) (0)
- 3H1458 NMR and Biological Studies of Anti-tumor Complex between Oleic Acid and Protein in the Molten Globule State(3H Protein: Property 5,The 49th Annual Meeting of the Biophysical Society of Japan) (2011) (0)
- Faculty Opinions recommendation of Single-molecule observation of protein-protein interactions in the chaperonin system. (2001) (0)
- Can we take a unified view of protein folding (2001) (0)
- Kinetic folding of lysozyme studied by time-resolved solution X-ray scattering (1999) (0)
- Analysis of stabilized recombinant goat α-lactalbumin mutants (1999) (0)
- 1PT160 Recognition of a TAR nucleic acid by HIV-1 Tat, an intrinsically disordered protein(The 50th Annual Meeting of the Biophysical Society of Japan) (2012) (0)
- Kinetic refolding of α-lactalbumin studied by stopped-flow X-ray scattering (2001) (0)
- 1P135 Experimental and simulation studies of the unfolding of recombinant and authentic lactalbumin : Effect of an N-terminal methionine residue (2004) (0)
- 1P131 Detection of substructural unfolding of SNase by intermolecular force microscopy(3. Protein folding and misfolding (1),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) (2006) (0)
- 3P-004 Single-molecule force-measurement of calcium ion effects on intramolecular structure of staphylococcal nuclease(The 46th Annual Meeting of the Biophysical Society of Japan) (2008) (0)
- 2P087 Analysis of Unfolding Transition of a Proline-free Variant of Staphylococcal Nuclease(Proteins-stability, folding, and other physicochemical properties,Poster Presentations) (2007) (0)
- 1P113 Backbone NMR assignment and hydrogen exchange of goat α-lactalbumin(3. Protein folding and misfolding (1),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) (2006) (0)
- 3P056 Structure of human α-lactalbumin in the transition state for folding (2005) (0)
- 1P071 The allosteric transition of GroEL in the presence of ADP(2. Protein function (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) (2006) (0)
- Interaction between the refolding intermediate of α-lactalbumin and a GroEL mutant (D398A) that lacks the ATPase activity (1999) (0)
- 1P014 Role of the Helical Protrusion of the Group II Chaperonin (2004) (0)
- Nucleotide-induced Structural Changes of GroEL Studied by X-ray Scattering (2001) (0)
- Temperature dependence of (A), the CD ellipticity at 230 nm (B) and the UV absorption at 340 nm (C) of MalZ at different scan rates. (2014) (0)
- 1P101 The role of Ca^ in the folding of goat α-Lactalbumin(3. Protein folding and misfolding (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) (2006) (0)
- Role of the interaction between ionizable groups in the folding of bovine alpha-lactalbumin. (1981) (0)
- Purification and folding study of canine milk lysozyme (2000) (0)
- 3P037 The unfolding simulation of goat α-lactalbumin (2005) (0)
- 3M1130 Roles of intermediate states in the folding of staphylococcal nuclease (2002) (0)
- Non-cooperative Nucleotide Binding to the E. coli Chaperonin GroEL. (1999) (0)
- Effect of GroEL on the refolding of staphylococcal nuclease (2003) (0)
- 1P079 Dissecting a bimolecular process of ATP binding to chaperonin GroEL(Protein:Function,The 48th Annual Meeting of the Biophysical Society of Japan) (2010) (0)
- Crystal structure of alpha-lactalbumin (2012) (0)
- Stabilization mechanism of goat alpha-lactalbumin mutants (2000) (0)
- 2P068 Effect of Ca2+ concentration on the stability and folding of canine milk lysozyme (2005) (0)
- Molecular mechanism of chaperonin function (2000) (0)
- PFDB: A standardized protein folding database with temperature correction (2019) (0)
- 1P039 Dynamic analysis of helical protrusion of group II chaperonins using fluorescent probes(Proteins-functions,Poster Presentations) (2007) (0)
- 2P059 Folding study of outer surface protein A(The 48th Annual Meeting of the Biophysical Society of Japan) (2010) (0)
- Equilibrium and kinetics of the unfolding of alpha-lactalbumin by guanidine hydrochloride (IV): dependence of the N equilibrium A transconformation on the temperature. (1977) (0)
- 2P111 Stochastic pathways and multiple intermediates of protein unfolding detected by single molecule measurements and MD simulation(Proteins-stability, folding, and other physicochemical properties,Poster Presentations) (2007) (0)
- 3P041 Structure of the transition state for folding of human α- lactalbumin (2004) (0)
- [Folding mechanism of protein]. (1994) (0)
- Analysis of the unfolding of authentic and recombinant a -lactalbumin : experiments and simulations (2003) (0)
- Folding Mechanisms of Homologous Proteins: A Comparative Study Between Lysozyme and a-Lactalbumin (2008) (0)
- 1H1548 Structural insights into the stability perturbations by N-terminal variations in human and goat α-lactalbumin(Protein: Property 2,The 49th Annual Meeting of the Biophysical Society of Japan) (2011) (0)
- Equilibrium and Kinetic Studies on Folding of the Authentic and Recombinant Forms of Human R-Lactalbumin by Circular Dichroism Spectroscopy † (0)
- Obsevation of unfolding straucturral changes of goat α-lactalbumin by molecular dynamics simulations at high temperature (1999) (0)
- 3P040 Acid Denaturation and Refolding of Green Fluorescent Protein (2004) (0)
- 1L600 Allosteric Transitions of GroEL Studied by Solution X-ray Scattering and Fluorescence Spectroscopy (2002) (0)
- Folding Mechanisms of Small Proteins GB1 and LB1 (2017) (0)
- 3P-020 Folding Mechanism of Homologous Proteins : A Comparative Study of Goat α-Lactalbumin and Canine Milk Lysozyme(The 46th Annual Meeting of the Biophysical Society of Japan) (2008) (0)
- 1P092 NMR resonance assignments and native-state hydrogen/deuterium exchange of a proline-free variant of staphylococcal nuclease (2005) (0)
- 2P057 The molten globule state and its biological function in α-lactalbumin(The 48th Annual Meeting of the Biophysical Society of Japan) (2010) (0)
- 1P-036 Structure and function of GroEL-GroES-nucleotide complexes studied by H/D exchange technique(Protein:Property, The 47th Annual Meeting of the Biophysical Society of Japan) (2009) (0)
- [The molecular mechanism of recognition of target proteins by GroEL]. (1996) (0)
- The interaction between the chaperonin mutant (D398A) and the target protein (2000) (0)
- Conformational changes induced by the disulfide bond reduction of bovine alpha -lactalbumin. (1980) (0)
- Faculty Opinions recommendation of Folding rates and low-entropy-loss routes of two-state proteins. (2003) (0)
- 1P082 The & phi- Value Analysis of Goat & alpha-Lactalbumin in the Absence of Calcium Ions (2005) (0)
- Correction to the article “Non‐native α‐helix formation is not necessary for folding of lipocalin: Comparison of burst‐phase folding between tear lipocalin and β‐lactoglobulin” (2009) (0)
- Formation of the chaperonin complex studied by 2D NMR spectroscopy (2017) (0)
- 3H1422 Dissecting a bimolecular process of ATP binding to the chaperonin GroEL(3H Protein: Property 5,The 49th Annual Meeting of the Biophysical Society of Japan) (2011) (0)
- 1SB51 Folding Mechanism of Proteins (2004) (0)
- 2D1648 Dynamic structural fluctuations of free heptameric GroES studied by hydrogen-exchange 2D NMR techniques(Protein: Structure & Function 1,The 48th Annual Meeting of the Biophysical Society of Japan) (2011) (0)
- 3P068 A theoretical study of unfolding pathway of Canine milk Iysozyme: Comparison with the unfolding pathway of Goat α-lactalbumin(Protein: Property,The 48th Annual Meeting of the Biophysical Society of Japan) (2010) (0)
- 1I1000 Cold denaturation of equine beta-lactoglobulin (2002) (0)
- THE AMYLOIDOGENIC PROPENSITY OF IMMUNOCLOBULIN LIGHT CHAIN YARIABLE (2014) (0)
- 1P105 Equilibrium and kinetics of the folding of canine milk lysozyme(3. Protein folding and misfolding (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) (2006) (0)
- 1999 XIII International Biophysics Congress 19-24 September 1999 New Delhi Abstracts Suppl (2016) (0)
- 2P093 The Native and Molten Globule States of Goat α-Lactalbumin Characterized by the NMR Hydrogen-exchange Technique(Proteins-stability, folding, and other physicochemical properties,Oral Presentations) (2007) (0)
- 3P064 Mutational analysis of protein solubility enhancement using short peptide tags(Proteins-stability, folding, and other physicochemical properties,Poster Presentations) (2007) (0)
- 1P040 Role of ATP hydrolysis in the cooperativity of subunits of group II chaperonins(Proteins-functions,Poster Presentations) (2007) (0)
- 3P066 The Stability and Folding/Unfolding of Staphylococcal Nuclease at the Residue Level(01C. Protein: Property,Poster) (2013) (0)
- 3M1115 Folding mechanism of staphylococcal nuclease mutants studied by a high-pressure temperature-jump apparatus (2002) (0)
- Contributory presentations/posters (1999) (0)
- An early immun~r~a~tiv~ folding intermediate of the trypt~phan synthase /I2 subunit is a 'molten globuk' (1990) (0)
- The B domain of protein A retains residual structures in 6 M guanidinium chloride as revealed by hydrogen/deuterium‐exchange NMR spectroscopy (2023) (0)
- 1P-026 The molten globule state and the biological function of α-lactalbumin(Protein:Structure & Function, The 47th Annual Meeting of the Biophysical Society of Japan) (2009) (0)
- Folding of green fluoresent protein (GFP) (1999) (0)
- Thermodynamic stability and kinetic folding of α-domain mutants of goat a-lactalbumin (2003) (0)
- 1P114 Folding mechanisms of a proline-free variant of staphylococcal nuclease studied by mutagenesis approach(3. Protein folding and misfolding (1),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) (2006) (0)
- 3P-013 Analysis of native-state prolyl isomerization of β2-microglobulin(The 46th Annual Meeting of the Biophysical Society of Japan) (2008) (0)
- Ca(2+)-induced secondary structural changes of troponin I. (2001) (0)
- Chaperonin-Affected Folding of Globular Proteins (2002) (0)
- Faculty Opinions recommendation of Structural characterization of an equilibrium unfolding intermediate in cytochrome c. (2006) (0)
- 1B1412 HD-exchange motion of free heptameric GroES studied by the use of TROSY and DMSO quenching followed by 2D NMR(Proteins: Structure & Function I,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan) (2012) (0)
- Protein engineering approach to the molten globule state of canime milk lysozyme. (1999) (0)
- 2P092 Equilibrium and kinetics of β_2-Microglobulin from the acid-unfolded state(Proteins-stability, folding, and other physicochemical properties,Oral Presentations) (2007) (0)
- 2PT150 Development of novel anti-tumor complexes made from a protein in the molten globule state(The 50th Annual Meeting of the Biophysical Society of Japan) (2012) (0)
- The folding mechanism of a(pro-)mutant of Staphylococcal nuclease studied by the pH-jump method (2001) (0)
- Secondary structure of SH3 domain in denatured state (2001) (0)
- The transition-state analysis of folding of alpha-lactalbumin (2001) (0)
- Statistical Analysis of the Relationship between the Folding Rate and Structure-Based Parameters of Globular Proteins (2006) (0)
- 3M1100 Refolding and unfolding of C-helix mutants of goat α-lactalbumin (2002) (0)
- 1PT143 THERMODYNAMIC PARAMETERS ASSOCIATED WITH THE GroEL-GroES BINDING(The 50th Annual Meeting of the Biophysical Society of Japan) (2012) (0)
- 1P038 Identification of the second ATP binding site of GroEL(Proteins-functions,Poster Presentations) (2007) (0)
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What Schools Are Affiliated With Kunihiro Kuwajima?
Kunihiro Kuwajima is affiliated with the following schools:
