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M Oobatake

Showing results (11-20 of 33) with videos related to

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Biophysical Chemistry|December 10, 1999
Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteinsM M Gromiha, M Oobatake, A Sarai
Journal of Biochemistry|November 1, 1985
Molecular orientation of plastocyanin on spinach thylakoid membranes as determined by acetylation of lysine residuesM Takano, M Takahashi, M Oobatake, et al.
Journal of Biotechnology|March 1, 1993
pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutionsS Kanaya, M Oobatake, H Nakamura, et al.
The Journal of Biological Chemistry|July 25, 1997
Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic coreA Akasako, M Haruki, M Oobatake, et al.
Biochemistry|May 23, 1995
Characterization of the internal motions of Escherichia coli ribonuclease HI by a combination of 15N-NMR relaxation analysis and molecular dynamics simulation: examination of dynamic modelsK Yamasaki, M Saito, M Oobatake, et al.
Biochemistry|June 27, 1995
High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradationA Akasako, M Haruki, M Oobatake, et al.
Biochimica Et Biophysica Acta|October 23, 1978
Flexibility of bovine pancreatic trypsin inhibitorT Ooi, K Nishikawa, M Oobatake, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1987
Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptidesT Ooi, M Oobatake, G Némethy, et al.
Biochemistry|December 26, 1995
Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR studyK Yamasaki, K Ogasahara, K Yutani, et al.
Protein Science : a Publication of the Protein Society|May 1, 1994
Thermodynamic characterization of an artificially designed amphiphilic alpha-helical peptide containing periodic prolines: observations of high thermal stability and cold denaturationE Kitakuni, Y Kuroda, M Oobatake, et al.
Pageof 4

Showing results (11-20 of 33) with videos related to

Sort By:
Pageof 4
Biophysical Chemistry|December 10, 1999
Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteinsM M Gromiha, M Oobatake, A Sarai
Journal of Biochemistry|November 1, 1985
Molecular orientation of plastocyanin on spinach thylakoid membranes as determined by acetylation of lysine residuesM Takano, M Takahashi, M Oobatake, et al.
Journal of Biotechnology|March 1, 1993
pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutionsS Kanaya, M Oobatake, H Nakamura, et al.
The Journal of Biological Chemistry|July 25, 1997
Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic coreA Akasako, M Haruki, M Oobatake, et al.
Biochemistry|May 23, 1995
Characterization of the internal motions of Escherichia coli ribonuclease HI by a combination of 15N-NMR relaxation analysis and molecular dynamics simulation: examination of dynamic modelsK Yamasaki, M Saito, M Oobatake, et al.
Biochemistry|June 27, 1995
High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradationA Akasako, M Haruki, M Oobatake, et al.
Biochimica Et Biophysica Acta|October 23, 1978
Flexibility of bovine pancreatic trypsin inhibitorT Ooi, K Nishikawa, M Oobatake, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1987
Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptidesT Ooi, M Oobatake, G Némethy, et al.
Biochemistry|December 26, 1995
Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR studyK Yamasaki, K Ogasahara, K Yutani, et al.
Protein Science : a Publication of the Protein Society|May 1, 1994
Thermodynamic characterization of an artificially designed amphiphilic alpha-helical peptide containing periodic prolines: observations of high thermal stability and cold denaturationE Kitakuni, Y Kuroda, M Oobatake, et al.
Pageof 4