K. Kuwajima

发表

Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy.

C. Matthews, K. Kuwajima, E. Garvey, 1991, Biochemistry.

Contribution of Thr29 to the thermodynamic stability of goat α‐lactalbumin as determined by experimental and theoretical approaches

K. Tsumoto, K. Kuwajima, M. Saito, 2001, Proteins.

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*

K. Maki, K. Kuwajima, M. Yohda, 2008, Journal of Biological Chemistry.

Determination of the structural ensemble of the molten globule state of a protein by computer simulations

Y. Okamoto, C. Dobson, K. Kuwajima, 2019, Proteins.

The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure

K. Kuwajima, K Kuwajima, 1989, Proteins.

Nature and locations of the most slowly exchanging peptide NH protons in residues 1 to 19 of ribonuclease S.

R. L. Baldwin, K. Kuwajima, 1983, Journal of molecular biology.

PFDB: A standardized protein folding database with temperature correction

Jooyoung Lee, Balachandran Manavalan, Kunihiro Kuwajima, 2019, Scientific Reports.

An early immunoreactive folding intermediate of the tryptophan synthase β2 subunit is a ‘molten globule’

S Sugai, O. Ptitsyn, B. Friguet, 1990, FEBS letters.

Role of the molten globule state in protein folding.

K. Kuwajima, M. Arai, Kunihiro Kuwajima, 2000, Advances in protein chemistry.

Atomically detailed description of the unfolding of alpha-lactalbumin by the combined use of experiments and simulations.

A. Kidera, M. Ikeguchi, K. Kuwajima, 2005, Journal of molecular biology.

Characterization of Archaeal Group II Chaperonin-ADP-Metal Fluoride Complexes

K. Maki, K. Kuwajima, T. Inobe, 2005, Journal of Biological Chemistry.

Chaperonin-Affected Folding of Globular Proteins

K. Kuwajima, T. Inobe, T. Makio, 2002, Journal of biological physics.

Effect of GroEL on the Re-folding Kinetics of α-Lactalbumin

K. Kuwajima, A. Okazaki, K. Katsumata, 1996 .

Role of the Helical Protrusion in the Conformational Change and Molecular Chaperone Activity of the Archaeal Group II Chaperonin*

K. Kuwajima, T. Inobe, M. Yohda, 2004, Journal of Biological Chemistry.

Experimental and Simulation Studies of the Folding/Unfolding of Goat α-Lactalbumin

A. Kidera, M. Ikeguchi, K. Kuwajima, 2009 .

Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry.

K. Kuwajima, K. Yutani, K. Ogasahara, 1992, Journal of molecular biology.

Equilibrium and kinetics of the folding and unfolding of canine milk lysozyme.

K. Maki, K. Kuwajima, S. Tomoda, 2007, Biochemistry.

Adaptation of a hyperthermophilic group II chaperonin to relatively moderate temperatures.

K. Kuwajima, M. Yohda, A. Yamagishi, 2010, Protein engineering, design & selection : PEDS.

Effect of GroEL on the re-folding kinetics of alpha-lactalbumin.

K. Kuwajima, A. Okazaki, K. Katsumata, 1996, Journal of molecular biology.

Oligomeric Hsp33 with Enhanced Chaperone Activity

K. Maki, K. Kuwajima, T. Inobe, 2004, Journal of Biological Chemistry.

Acid denaturation and refolding of green fluorescent protein.

K. Maki, K. Kuwajima, K. Saeki, 2004, Biochemistry.

The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins

K. Kuwajima, 2020, Biomolecules.

Sequential four‐state folding/unfolding of goat α‐lactalbumin and its N‐terminal variants

K. Makabe, K. Maki, K. Kuwajima, 2012, Proteins.

Fibrillogenic propensity of the GroEL apical domain: A Janus‐faced minichaperone

M. Vendruscolo, K. Makabe, K. Kuwajima, 2012, FEBS letters.

Water and Biomolecules

Mikio Kataoka, Yuji Goto, Masahide Terazima, 2009 .

Helical and expanded conformation of equine beta-lactoglobulin in the cold-denatured state.

Y. Amemiya, K. Kuwajima, M. Arai, 2005, Journal of molecular biology.

DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science

K. Kuwajima, M. Yagi-Utsumi, S. Yanaka, 2022, Molecules.

Parallel folding pathway of proline-free staphylococcal nuclease studied by the stopped-flow double-jump method

K. Kuwajima, K. Kamagata, 2003 .

The Pro117 to glycine mutation of staphylococcal nuclease simplifies the unfolding—folding kinetics

K. Kuwajima, S. Sugai, Kaori Yamamoto, 1991, FEBS letters.

Kinetic refolding of α-lactalbumin studied by stopped-flow X-ray scattering

Y. Amemiya, K. Maki, K. Kuwajima, 2001 .

Solution X-ray scattering study on the chaperonin GroEL from Escherichia coli.

K. Kuwajima, T. Ikura, H. Kihara, 1995, Biophysical chemistry.

Innocuous character of [ethylenebis(oxyethylenenitrilo)]tetraacetic acid and EDTA as metal-ion buffers in studying Ca2+ binding by alpha-lactalbumin.

K. Kuwajima, S. Sugai, Y. Harushima, 1986, The Journal of biological chemistry.

Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy.

K. Kuwajima, M. Arai, M. Mizuguchi, 1998, Journal of molecular biology.

Application of the pH-jump method to the titration of tyrosine residues in bovine alpha-lactalbumin.

K. Kuwajima, S. Sugai, Y. Ogawa, 1979, Biochemistry.

Experimental studies of folding kinetics and structural dynamics of small proteins.

K. Kuwajima, F. Schmid, K Kuwajima, 1984, Advances in biophysics.

Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin.

K. Kuwajima, S. Sugai, Y. Hiraoka, 1985, Biochemistry.

Rapid formation of a molten globule intermediate in refolding of α-lactalbumin

K. Kuwajima, M. Arai, 1996 .

The molten globule state of α‐lactalbumin

K. Kuwajima, 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Effects of amino acid substitutions in the hydrophobic core of alpha-lactalbumin on the stability of the molten globule state.

K. Kuwajima, K. Watanabe, I. Kumagai, 1995, Protein engineering.

Unfolding pathways of goat alpha-lactalbumin as revealed in multiple alignment of molecular dynamics trajectories.

M. Ota, A. Kidera, M. Ikeguchi, 2007, Journal of molecular biology.

α-Lactalbumin: A calcium metalloprotein

K. Kuwajima, S. Sugai, Y. Hiraoka, 1980 .

Exchange behavior of the H-bonded amide protons in the 3 to 13 helix of ribonuclease S.

R. L. Baldwin, K. Kuwajima, 1983, Journal of molecular biology.

Stopped-Flow Circular Dichroism

K. Kuwajima, 1996 .

Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism

S Sugai, K. Kuwajima, S. Sugai, 1987, FEBS letters.

Equilibrium and kinetics of the thermal unfolding of alpha-lactalbumin. The relation to its folding mechanism.

K. Kuwajima, S. Sugai, 1978, Biophysical chemistry.

Influence of Ca2+ binding on the structure and stability of bovine alpha-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra.

K. Kuwajima, S. Sugai, Y. Harushima, 2009, International journal of peptide and protein research.

Ca2+-induced alteration in the unfolding behavior of alpha-lactalbumin.

K. Kuwajima, S. Sugai, M. Ikeguchi, 1986, Journal of biochemistry.

Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein.

K. Kuwajima, T. Ikura, I. Kumagai, 1999, Protein engineering.

Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli.

K. Tsumoto, K. Kuwajima, T. Ikura, 1999, Journal of Molecular Biology.

An Overlapping Region between the Two Terminal Folding Units of the Outer Surface Protein A (OspA) Controls Its Folding Behavior.

K. Makabe, S. Koide, K. Kuwajima, 2018, Journal of molecular biology.

The use of spin desalting columns in DMSO‐quenched H/D‐exchange NMR experiments

K. Kuwajima, Jin Chen, Koichi Kato, 2013, Protein science : a publication of the Protein Society.

The H/D-exchange kinetics of the Escherichia coli co-chaperonin GroES studied by 2D NMR and DMSO-quenched exchange methods.

K. Makabe, K. Kuwajima, A. Mukaiyama, 2013, Journal of molecular biology.

NMR characterization of the interaction of GroEL with amyloid β as a model ligand

K. Makabe, K. Kuwajima, Yoshinori Uekusa, 2013, FEBS letters.

Folding of green fluorescent protein and the cycle3 mutant.

K. Kuwajima, M. Arai, K Kuwajima, 2000, Biochemistry.

Irreversible Denaturation of Maltodextrin Glucosidase Studied by Differential Scanning Calorimetry, Circular Dichroism, and Turbidity Measurements

K. Kuwajima, T. Chaudhuri, M. Goyal, 2014, PloS one.

Formation of the chaperonin complex studied by 2D NMR spectroscopy

S. Paul, K. Makabe, K. Kuwajima, 2017, PloS one.

The equilibrium unfolding intermediate observed at pH 4 and its relationship with the kinetic folding intermediates in green fluorescent protein.

K. Maki, K. Kuwajima, K. Kamagata, 2006, Journal of molecular biology.

Denaturation and reassembly of chaperonin GroEL studied by solution X‐ray scattering

Y. Amemiya, K. Maki, K. Kuwajima, 2003, Protein science : a publication of the Protein Society.

Chaperonin-affected refolding of alpha-lactalbumin: effects of nucleotides and the co-chaperonin GroES.

K. Kuwajima, M. Arai, T. Makio, 1999, Journal of molecular biology.

Solubilization and folding of a fully active recombinant Gaussia luciferase with native disulfide bonds by using a SEP-Tag.

K. Kuwajima, M. Yohda, Y. Kuroda, 2011, Biochimica et biophysica acta.

Is folding of β-lactoglobulin non-hierarchic? intermediate with native-like β-sheet and non-native α-helix

C. Batt, K. Kuwajima, M. Arai, 2000 .

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.

K. Kuwajima, S. Sugai, M. Ikeguchi, 1986, Biochemistry.

Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy.

Y. Amemiya, K. Kuwajima, T. Ikura, 1998, Journal of molecular biology.

Kinetics of disulfide bond reduction in alpha-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond.

K. Kuwajima, S. Sugai, T. Sugawara, 1990, Biochemistry.

Antitumor Complexes Formed by Oleic Acid and Molten Globule Intermediates of Proteins

Takashi Nakamura, K. Kuwajima, 2016 .

Molecular Mechanisms of the Cytotoxicity of Human α-Lactalbumin Made Lethal to Tumor Cells (HAMLET) and Other Protein-Oleic Acid Complexes*

K. Makabe, Takashi Nakamura, K. Kuwajima, 2013, The Journal of Biological Chemistry.

Characterization of the critical state in protein folding. Effects of guanidine hydrochloride and specific Ca2+ binding on the folding kinetics of alpha-lactalbumin.

K. Kuwajima, S. Sugai, M. Mitani, 1989, Journal of molecular biology.

A folding model of α-lactalbumin deduced from the three-state denaturation mechanism

K. Kuwajima, 1977 .

Three-state denaturation of α-lactalbumin by guanidine hydrochloride

K. Kuwajima, S. Sugai, K. Nitta, 1976 .

Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase.

C. Matthews, K. Kuwajima, M. Arai, 2003, Journal of molecular biology.

Detection and characterization of the intermediate on the folding pathway of human alpha-lactalbumin.

K. Kuwajima, S. Sugai, K. Nitta, 1978, Biochemistry.

Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.

K. Kuwajima, T. Inobe, T. Makio, 2001, Biochimica et biophysica acta.

Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: evidence for noncooperative nucleotide binding.

K. Kuwajima, T. P. Terada, 1999, Biochimica et biophysica acta.

Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding.

Masasuke Yoshida, K. Kuwajima, M. Yoshida, 2000, Biochemical and biophysical research communications.

Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL.

K. Kuwajima, T. Ikura, G. Tsurupa, 1998, Journal of molecular biology.

Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry

K. Kuwajima, Jin Chen, Qian Zhang, 2013, Scientific Reports.

Phi value analysis of an allosteric transition of GroEL based on a single-pathway model.

K. Kuwajima, T. Inobe, 2004, Journal of molecular biology.

The allosteric transition of GroEL induced by metal fluoride-ADP complexes.

K. Kuwajima, T. Inobe, M. Arai, 2003, Journal of molecular biology.

Asymmetry of the GroEL-GroES complex under physiological conditions as revealed by small-angle x-ray scattering.

K. Maki, K. Kuwajima, K. Kamagata, 2008, Biophysical journal.

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.

K. Kuwajima, T. Makio, E. Takasu-Ishikawa, 2001, Journal of molecular biology.

The use of the time-resolved X-ray solution scattering for studies of globular proteins

Y. Amemiya, K. Maki, K. Kuwajima, 2002 .

The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state

K. Kuwajima, T. Ikura, A. Okazaki, 1994, Nature Structural Biology.

Dominant Forces in the Recognition of a Transient Folding Intermediate of α-Lactalbumin by GroEL

K. Kuwajima, A. Okazaki, G. Tsurupa, 1996 .

Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL.

K. Kuwajima, A. Okazaki, G. Tsurupa, 1996, Journal of molecular biology.

ATP Dependent Rotational Motion of Group II Chaperonin Observed by X-ray Single Molecule Tracking

K. Makabe, K. Kuwajima, M. Yohda, 2013, PloS one.

The molten globule of β(2)-microglobulin accumulated at pH 4 and its role in protein folding.

K. Makabe, K. Maki, K. Kuwajima, 2013, Journal of molecular biology.

Exploring the Folding Mechanism of Small Proteins GB1 and LB1.

K. Kuwajima, Juyong Lee, InSuk Joung, 2019, Journal of chemical theory and computation.

Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride (IV) Dependence of the N ⇌ A transconformation on temperature

K. Kuwajima, S. Sugai, K. Nitta, 1977 .

Hydrogen exchange of the tryptophan residues in bovine α‐lactalbumin studied by uv spectroscopy

K. Kuwajima, S. Sugai, Y. Harushima, 1988 .

Structural characterization of the molten globule of α‐lactalbumin by solution X‐ray scattering

K. Kuwajima, M. Kataoka, Y. Goto, 1997, Protein science : a publication of the Protein Society.

Folding of staphylococcal nuclease A studied by equilibrium and kinetic circular dichroism spectra.

K. Kuwajima, S. Sugai, T. Sugawara, 1991, Biochemistry.

Transition state in the folding of α‐lactalbumin probed by the 6‐120 disulfide bond

K. Kuwajima, S. Sugai, Masao Kato, 1998, Protein science : a publication of the Protein Society.

Native-state heterogeneity of β(2)-microglobulin as revealed by kinetic folding and real-time NMR experiments.

K. Makabe, K. Maki, K. Kuwajima, 2013, Journal of molecular biology.

Fast folding of Escherichia coli cyclophilin A: a hypothesis of a unique hydrophobic core with a phenylalanine cluster.

K. Kuwajima, N. Takahashi, T. Ikura, 2000, Journal of molecular biology.

The B domain of protein A retains residual structures in 6 M guanidinium chloride as revealed by hydrogen/deuterium‐exchange NMR spectroscopy

K. Kuwajima, M. Yagi-Utsumi, S. Yanaka, 2023, Protein science : a publication of the Protein Society.

Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR

K. Kuwajima, Takumi Yamaguchi, Koichi Kato, 2018, bioRxiv.

Unification of the folding mechanisms of non-two-state and two-state proteins.

Munehito Arai, Kunihiro Kuwajima, Kiyoto Kamagata, 2004, Journal of molecular biology.

PFDB: A standardized protein folding database with temperature correction

Balachandran Manavalan, Jooyoung Lee, K. Kuwajima, 2019, Scientific Reports.

Mutational analysis of protein solubility enhancement using short peptide tags.

K. Maki, K. Kuwajima, K. Soda, 2007, Biopolymers.

Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin.

K. Kuwajima, M. Arai, 1996, Folding & design.

Different folding pathways taken by highly homologous proteins, goat alpha-lactalbumin and canine milk lysozyme.

K. Makabe, K. Maki, K. Kuwajima, 2010, Journal of molecular biology.

Dissecting a bimolecular process of MgATP²- binding to the chaperonin GroEL.

K. Makabe, K. Kuwajima, Jin Chen, 2011, Journal of molecular biology.

Protein globularization during folding. A study by synchrotron small-angle X-ray scattering.

Y. Amemiya, K. Wakabayashi, K. Kuwajima, 1996, Journal of Molecular Biology.

Thermodynamic characterization of partially denatured states in the denaturation process of bovine alpha-lactalbumin by inorganic denaturants.

K. Kuwajima, S. Sugai, S. Maruyama, 1977, Biochimica et biophysica acta.

Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride (II)

K. Kuwajima, S. Sugai, K. Nitta, 1976 .

The Catalytic Domain of Topological Knot tRNA Methyltransferase (TrmH) Discriminates between Substrate tRNA and Nonsubstrate tRNA via an Induced-fit Process*

O. Nureki, K. Makabe, K. Kuwajima, 2013, The Journal of Biological Chemistry.

Flexible Recognition of the tRNA G18 Methylation Target Site by TrmH Methyltransferase through First Binding and Induced Fit Processes*

K. Makabe, K. Kuwajima, A. Ochi, 2010, The Journal of Biological Chemistry.

Reversible and fast association equilibria of a molecular chaperone, gp57A, of bacteriophage T4.

K. Kuwajima, M. Arai, S. Kidokoro, 2003, Biophysical journal.

Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human α-lactalbumin by circular dichroism spectroscopy

K. Kuwajima, T. Ikura, M. Arai, 2000 .

Structural insights into the stability perturbations induced by N-terminal variation in human and goat α-lactalbumin.

K. Makabe, K. Kuwajima, Takashi Nakamura, 2013, Protein engineering, design & selection : PEDS.

Localized Nature of the Transition-state Structure in Goat α-Lactalbumin Folding

K. Kuwajima, T. Yoda, M. Arai, 2004 .

Folding-unfolding equilibrium and kinetics of equine beta-lactoglobulin: equivalence between the equilibrium molten globule state and a burst-phase folding intermediate.

K. Kuwajima, S. Sugai, M. Arai, 1999, Biochemistry.

Contribution of the 6-120 disulfide bond of alpha-lactalbumin to the stabilities of its native and molten globule states.

K. Kuwajima, S. Sugai, T. Sugawara, 1992, Biochemistry.

Hydrogen exchange study of canine milk lysozyme: Stabilization mechanism of the molten globule

K. Kuwajima, M. Demura, K. Nitta, 2000, Proteins.

Calcium-regulated interactions of human α-lactalbumin with bee venom melittin

K. Kuwajima, S. Sugai, E. Permyakov, 1991 .

Calcium-regulated interactions of human alpha-lactalbumin with bee venom melittin.

K. Kuwajima, S. Sugai, E. Permyakov, 1991, Biophysical Chemistry.

Structure and thermodynamics of the extraordinarily stable molten globule state of canine milk lysozyme.

I. Tanaka, M. Yao, K. Kuwajima, 2000, Biochemistry.

ErratumErratum to “Unification of the Folding Mechanisms of Non-two-state and Two-state Proteins” [J. Mol. Biol. (2004) 339, 951–965]

K. Kuwajima, K. Kamagata, M. Arai, 2004 .

Folding mechanism of canine milk lysozyme studied by circular dichroism and fluorescence spectroscopy

K. Kuwajima, M. Arai, K. Nitta, 2003 .

Purification and folding study of canine milk lysozyme

K. Kuwajima, M. Arai, K. Nitta, 2000 .

Three-state denaturation of alpha-lactalbumin by guanidine hydrochloride.

K. Kuwajima, S. Sugai, K. Nitta, 1976, Journal of molecular biology.

Protein folding in vitro.

K. Kuwajima, 1992, Current opinion in biotechnology.

Characterization of kinetic folding intermediates of recombinant canine milk lysozyme by stopped-flow circular dichroism.

K. Maki, K. Kuwajima, M. Arai, 2005, Biochemistry.

Non‐native α‐helix formation is not necessary for folding of lipocalin: Comparison of burst‐phase folding between tear lipocalin and β‐lactoglobulin

K. Maki, K. Kuwajima, H. Tsuge, 2009, Proteins.

The burst-phase intermediate in the refolding of beta-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy.

K. Kuwajima, S. Sugai, H. Yamaya, 1996, Journal of molecular biology.

Intramolecular perturbation of tryptophans induced by the protonation of ionizable groups in goat alpha-lactalbumin.

K. Kuwajima, S. Sugai, K. Nitta, 1980, Biochimica et biophysica acta.

Dissection of the ATP-dependent conformational change cycle of a group II chaperonin.

K. Makabe, K. Kuwajima, M. Yohda, 2014, Journal of molecular biology.

Multiple parallel-pathway folding of proline-free Staphylococcal nuclease.

Kunihiro Kuwajima, Kiyoto Kamagata, Masaru Tanokura, 2003, Journal of molecular biology.

Effects of proline mutations on the folding of staphylococcal nuclease.

K. Maki, K. Kuwajima, N. Takahashi, 1999, Biochemistry.

Solvent environments significantly affect the enzymatic function of Escherichia coli dihydrofolate reductase: comparison of wild-type protein and active-site mutant D27E.

K. Gekko, K. Kuwajima, E. Ohmae, 2013, Biochimica et biophysica acta.

Fast Compaction of α-Lactalbumin During Folding Studied by Stopped-flow X-ray Scattering

Y. Amemiya, K. Maki, K. Kuwajima, 2002 .

Kinetic folding and unfolding of staphylococcal nuclease and its six mutants studied by stopped‐flow circular dichroism

K. Kuwajima, Nikolay N. Kalnin, 1995, Proteins.

Folding of carp parvalbumin studied by equilibrium and kinetic circular dichroism spectra

K. Kuwajima, S. Sugai, A. Sakuraoka, 1988 .

Folding‐unfolding of goat α‐lactalbumin studied by stopped‐flow circular dichroism and molecular dynamics simulations

K. Tsumoto, K. Kuwajima, M. Saito, 2001, Proteins.

The allosteric transition of the chaperonin groel fromescherichia coli as studied by solution X-ray scattering

K. Kuwajima, T. Inobe, M. Arai, 2006 .

Solubilization and folding of a fully active recombinant Gaussia luciferase with native disulfide bonds by using a SEP-Tag.

K. Kuwajima, M. Yohda, Y. Kuroda, 2011, Biochimica et biophysica acta.

Dissecting a bimolecular process of MgATP²- binding to the chaperonin GroEL.

K. Makabe, K. Kuwajima, Jin Chen, 2011, Journal of molecular biology.

Effect of an alternative disulfide bond on the structure, stability, and folding of human lysozyme.

K. Kuwajima, E. Kanaya, M. Arai, 2000, Biochemistry.

Equilibrium and Kinetic Studies on Folding of the Authentic and Recombinant Forms of Human R-Lactalbumin by Circular Dichroism Spectroscopy †

K. Kuwajima, T. Ikura, M. Arai, 2022 .

Electrophoretic investigations of the acid conformational change of alpha-lactalbumin.

K. Kuwajima, S. Sugai, K. Nitta, 1975, Journal of biochemistry.

Molecular Mechanisms of the Cytotoxicity of Human α-Lactalbumin Made Lethal to Tumor Cells (HAMLET) and Other Protein-Oleic Acid Complexes*

K. Makabe, Takashi Nakamura, K. Kuwajima, 2013, The Journal of Biological Chemistry.

alpha-Lactalbumin: a calcium metalloprotein.

K. Kuwajima, S. Sugai, Y. Hiraoka, 1980, Biochemical and biophysical research communications.

Probing force-induced unfolding intermediates of a single staphylococcal nuclease molecule and the effect of ligand binding.

Yoshihiro Murayama, Masaki Sano, Kunihiro Kuwajima, 2008, Biochemical and biophysical research communications.

Strategy for trapping intermediates in the folding of ribonuclease and for using 1H‐NMR to determine their structures

P S Kim, P. S. Kim, R. L. Baldwin, 1983, Biopolymers.

Contributory presentations/posters

Diederichs, Bosco K. Ho, Hironori K. Nakamura, 1999, Journal of Biosciences.

Obsevation of unfolding straucturral changes of goat α-lactalbumin by molecular dynamics simulations at high temperature

K. Tsumoto, K. Kuwajima, M. Saito, 1999 .

Role of the Interaction between Ionizable Groups in the Folding of Bovine α-Lactalbumin

K. Kuwajima, S. Sugai, Y. Ogawa, 1981 .

Structure-based protein folding type classification and folding rate prediction

Jooyoung Lee, Balachandran Manavalan, InSuk Joung, 2015, 2015 IEEE International Conference on Bioinformatics and Biomedicine (BIBM).

Surprisingly high correlation between early and late stages in non-two-state protein folding.

Kunihiro Kuwajima, Kiyoto Kamagata, K. Kuwajima, 2006, Journal of molecular biology.

Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR.

K. Kuwajima, Koichi Kato, M. Yagi-Utsumi, 2020, Biophysical journal.