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

B T Nall

Showing results (1-10 of 40) with videos related to

Pageof 4
Sort By:
Biochemistry|March 15, 1983
Structural intermediates in folding of yeast iso-2 cytochrome cB T Nall
Biochemistry|May 20, 1986
Native or nativelike species are transient intermediates in folding of alkaline iso-2 cytochrome cB T Nall
Biochemistry|May 14, 1991
Effective concentrations of amino acid side chains in an unfolded proteinK Muthukrishnan, B T Nall
Biochemistry|January 25, 1994
Characterization of folding intermediates using prolyl isomeraseS Veeraraghavan, B T Nall
Biochemistry|November 4, 1986
Folding/unfolding kinetics of mutant forms of iso-1-cytochrome c with replacement of proline-71L Ramdas, B T Nall
Journal of Molecular Biology|May 10, 2000
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerizationM M Pierce, B T Nall
Biochemistry|December 31, 1985
Slow refolding kinetics in yeast iso-2 cytochrome cJ J Osterhout, B T Nall
Protein Science : a Publication of the Protein Society|March 1, 1997
Fast folding of cytochrome cM M Pierce, B T Nall
Biochemistry|August 21, 1990
Rates and energetics of tyrosine ring flips in yeast iso-2-cytochrome cB T Nall, E H Zuniga
Biochemistry|March 15, 1983
Folding of yeast iso-1-AM cytochrome cE H Zuniga, B T Nall
Pageof 4

Showing results (1-10 of 40) with videos related to

Sort By:
Pageof 4
Biochemistry|March 15, 1983
Structural intermediates in folding of yeast iso-2 cytochrome cB T Nall
Biochemistry|May 20, 1986
Native or nativelike species are transient intermediates in folding of alkaline iso-2 cytochrome cB T Nall
Biochemistry|May 14, 1991
Effective concentrations of amino acid side chains in an unfolded proteinK Muthukrishnan, B T Nall
Biochemistry|January 25, 1994
Characterization of folding intermediates using prolyl isomeraseS Veeraraghavan, B T Nall
Biochemistry|November 4, 1986
Folding/unfolding kinetics of mutant forms of iso-1-cytochrome c with replacement of proline-71L Ramdas, B T Nall
Journal of Molecular Biology|May 10, 2000
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerizationM M Pierce, B T Nall
Biochemistry|December 31, 1985
Slow refolding kinetics in yeast iso-2 cytochrome cJ J Osterhout, B T Nall
Protein Science : a Publication of the Protein Society|March 1, 1997
Fast folding of cytochrome cM M Pierce, B T Nall
Biochemistry|August 21, 1990
Rates and energetics of tyrosine ring flips in yeast iso-2-cytochrome cB T Nall, E H Zuniga
Biochemistry|March 15, 1983
Folding of yeast iso-1-AM cytochrome cE H Zuniga, B T Nall
Pageof 4