Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

K Gekko

Showing results (21-30 of 39) with videos related to

Pageof 4
Sort By:
Journal of Biochemistry|September 1, 2001
Effects of five-tryptophan mutations on structure, stability and function of Escherichia coli dihydrofolate reductaseE Ohmae, Y Sasaki, K Gekko
Bioscience, Biotechnology, and Biochemistry|July 5, 2016
Competing Effect of Polyols on the Thermal Stability and Gelation of Soy ProteinK Gekko, X Li, S Makino
Methods in Enzymology|January 1, 1979
Measurements of preferential solvent interactions by densimetric techniquesJ C Lee, K Gekko, S N Timasheff
Journal of Biochemistry|July 6, 2000
Single amino acid substitutions in flexible loops can induce large compressibility changes in dihydrofolate reductaseK Gekko, T Kamiyama, E Ohmae, et al.
Journal of Biochemistry|March 21, 1998
Nonadditive effects of double mutations at the flexible loops, glycine-67 and glycine-121, of Escherichia coli dihydrofolate reductase on its stability and functionE Ohmae, K Iriyama, S Ichihara, et al.
Biochimica Et Biophysica Acta|November 11, 1999
Polyol-induced molten globule of cytochrome c: an evidence for stabilization by hydrophobic interactionT Kamiyama, Y Sadahide, Y Nogusa, et al.
Biochimica Et Biophysica Acta|September 28, 1998
Acetonitrile-protein interactions: amino acid solubility and preferential solvationK Gekko, E Ohmae, K Kameyama, et al.
Journal of Biochemistry|June 19, 1998
Effects of point mutations at the flexible loop alanine-145 of Escherichia coli dihydrofolate reductase on its stability and functionE Ohmae, K Ishimura, M Iwakura, et al.
Journal of Biochemistry|November 1, 1996
Acid and thermal unfolding of Escherichia coli dihydrofolate reductaseE Ohmae, T Kurumiya, S Makino, et al.
Journal of Biochemistry|April 1, 1996
Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and functionE Ohmae, K Iriyama, S Ichihara, et al.
Pageof 4

Showing results (21-30 of 39) with videos related to

Sort By:
Pageof 4
Journal of Biochemistry|September 1, 2001
Effects of five-tryptophan mutations on structure, stability and function of Escherichia coli dihydrofolate reductaseE Ohmae, Y Sasaki, K Gekko
Bioscience, Biotechnology, and Biochemistry|July 5, 2016
Competing Effect of Polyols on the Thermal Stability and Gelation of Soy ProteinK Gekko, X Li, S Makino
Methods in Enzymology|January 1, 1979
Measurements of preferential solvent interactions by densimetric techniquesJ C Lee, K Gekko, S N Timasheff
Journal of Biochemistry|July 6, 2000
Single amino acid substitutions in flexible loops can induce large compressibility changes in dihydrofolate reductaseK Gekko, T Kamiyama, E Ohmae, et al.
Journal of Biochemistry|March 21, 1998
Nonadditive effects of double mutations at the flexible loops, glycine-67 and glycine-121, of Escherichia coli dihydrofolate reductase on its stability and functionE Ohmae, K Iriyama, S Ichihara, et al.
Biochimica Et Biophysica Acta|November 11, 1999
Polyol-induced molten globule of cytochrome c: an evidence for stabilization by hydrophobic interactionT Kamiyama, Y Sadahide, Y Nogusa, et al.
Biochimica Et Biophysica Acta|September 28, 1998
Acetonitrile-protein interactions: amino acid solubility and preferential solvationK Gekko, E Ohmae, K Kameyama, et al.
Journal of Biochemistry|June 19, 1998
Effects of point mutations at the flexible loop alanine-145 of Escherichia coli dihydrofolate reductase on its stability and functionE Ohmae, K Ishimura, M Iwakura, et al.
Journal of Biochemistry|November 1, 1996
Acid and thermal unfolding of Escherichia coli dihydrofolate reductaseE Ohmae, T Kurumiya, S Makino, et al.
Journal of Biochemistry|April 1, 1996
Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and functionE Ohmae, K Iriyama, S Ichihara, et al.
Pageof 4