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Chemistry

D-Index
49
Citations
12082
World Ranking
14659
National Ranking
1144

Overview

Kunihiro Kuwajima is affiliated with Tokyo University of Science in Japan and specializes in research within the fields of Biochemistry, Genetics and Molecular Biology, and Materials Science. Their work primarily focuses on protein structure and dynamics, enzyme structure and function, and the application of advanced nuclear magnetic resonance (NMR) techniques.

The scientist's recent publications cover a range of topics related to protein folding, residual protein structures, and specialized NMR spectroscopy methods. Notable papers include:

  • The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins, 2020, Biomolecules
  • The Molten Globule, and Two-State vs. Non-Two-State Folding of Globular Proteins, 2020, Preprints.org
  • DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science, 2022, Molecules
  • Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR, 2020, Biophysical Journal
  • The B domain of protein A retains residual structures in 6 M guanidinium chloride as revealed by hydrogen/deuterium-exchange NMR spectroscopy, 2023, Protein Science

Kuwajima has collaborated frequently with researchers including Maho Yagi-Utsumi, Saeko Yanaka, Koichi Kato, Mahesh Chandak, and Methanee Hiranyakorn.

Their research spans several subfields such as Molecular Biology, Materials Chemistry, Food Science, and Spectroscopy. Key research topics include:

  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Proteins in Food Systems
  • Advanced NMR Techniques and Applications
  • Glycosylation and Glycoproteins Research
  • Mass Spectrometry Techniques and Applications

Frequent publication venues for Kuwajima's work include Biomolecules, Molecules, Preprints.org, Biophysical Journal, and Protein Science.

Best Publications

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

    Kunihiro Kuwajima

  • The molten globule state of alpha-lactalbumin.

    Kunihiro Kuwajima

  • Role of the molten globule state in protein folding.

    Munehito Arai;Kunihiro Kuwajima

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

    Kunihiro Kuwajima;Yoshiki Hiraoka;Masamichi Ikeguchi;Shintaro Sugai

  • α-Lactalbumin: A calcium metalloprotein

    Yoshiki Hiraoka;Tatsuhisa Segawa;Kunihiro Kuwajima;Shintaro Sugai

  • 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.

    Masamichi Ikeguchi;Kunihiro Kuwajima;Masahiro Mitani;Shintaro Sugai

  • Three-state denaturation of α-lactalbumin by guanidine hydrochloride

    Kunihiro Kuwajima;Katsutoshi Nitta;Michio Yoneyama;Shintaro Sugai

  • Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism.

    Kunihiro Kuwajima;Hidetoshi Yamaya;Soichi Miwa;Shintaro Sugai

  • Folding of green fluorescent protein and the cycle3 mutant.

    Hiroyuki Fukuda;Munehito Arai;Kunihiro Kuwajima

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

    Kunihiro Kuwajima;Masahiro Mitani;Shintaro Sugai

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

    Kunihiro Kuwajima

  • Protein Globularization During Folding. A Study by Synchrotron Small-angle X-ray Scattering

    Gennady V. Semisotnov;Hiroshi Kihara;Nina V. Kotova;Kazumoto Kimura

  • Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering.

    M. Kataoka;K. Kuwajima;F. Tokunaga;Y. Goto

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

    Munehito Arai;Kunihiro Kuwajima

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

    Masamichi Ikeguchi;Kunihiro Kuwajima;Shintaro Sugai

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

    Kunihiro Kuwajima;Masamichi Ikeguchi;Tatsuro Sugawara;Yoshiki Hiraoka

  • The Burst-phase Intermediate in the Refolding of β-Lactoglobulin Studied by Stopped-flow Circular Dichroism and Absorption Spectroscopy

    Kunihiro Kuwajima;Hidetoshi Yamaya;Hidetoshi Yamaya;Shintaro Sugai;Shintaro Sugai

  • Absence of the thermal transition in apo-α-lactalbumin in the molten globule state: A study by differential scanning microcalorimetry☆

    Katsuhide Yutani;Kyoko Ogasahara;Kunihiro Kuwajima

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

    Munehito Arai;Teikichi Ikura;Gennady V Semisotnov;Hiroshi Kihara

  • Acid denaturation and refolding of green fluorescent protein.

    Sawako Enoki;Kimiko Saeki;Kosuke Maki;Kunihiro Kuwajima

Frequent Co-Authors

Koichi Kato
Koichi Kato National Institutes of Natural Sciences
Masafumi Yohda
Masafumi Yohda Tokyo University of Agriculture and Technology
Takashi Nakamura
Takashi Nakamura Kyoto University
Yuji Goto
Yuji Goto Osaka University
Izumi Kumagai
Izumi Kumagai Tokyo University of Agriculture and Technology
Kouhei Tsumoto
Kouhei Tsumoto University of Tokyo
Seiji Okada
Seiji Okada Kumamoto University
Gabor Tigyi
Gabor Tigyi University of Tennessee Health Science Center
Mikio Kataoka
Mikio Kataoka Nara Institute of Science and Technology
Christoph Schick
Christoph Schick University of Rostock

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