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Kinetic study on the unfolding of apomyoglobin, detected by fluorescence- and circular dichroism-stopped-flow method

  • Published:1980-08 Issue:4 Volume:95 Page:1687-1694
  • ISSN:0006-291X
  • Container-title:Biochemical and Biophysical Research Communications
  • language:en
  • Short-container-title:Biochemical and Biophysical Research Communications

Author:

Kihara Hiroshi,Takahashi Etsuko,Yamamura Kazuo,Tabushi Iwao

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference10 articles.

1. Ohgushi, M., Kihara, H., and Takahashi, E., in preparation.

2. Studies on the structure of hemoglobin I. Physicochemical properties of human globin

3. Reversible Conformational Changes of Myoglobin and Apomyoglobin

4. Protein, Nucleic Acid and Enzyme;Ohta,1974

5. Kihara, H., Takahashi, E., Yamamura, K., and Tabushi, I., in preparation.

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1. Spectroscopic study on acid-induced unfolding and refolding of apo-neuroglobin;Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy;2010-05

2. Kinetic studies of unfolding process of aspergillopepsin II by pH-jump methods;Biochemical and Biophysical Research Communications;2003-02

3. Myoglobin-NO at Low pH: Free Four-Coordinated Heme in the Protein Pocket;Biochemistry;1995-02-28

4. Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods;Proteins: Structure, Function, and Genetics;1994-06

5. THE H-HELIX OF MYOGLOBIN AS A POTENTIAL INDEPENDENT PROTEIN FOLDING DOMAIN;Current Research in Protein Chemistry;1990
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