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 M Moreton

Showing results (1-10 of 8) with videos related to

Pageof 1
Sort By:
Protein Engineering|October 1, 1992
The structural consequences of exchanging tryptophan and tyrosine residues in B. stearothermophilus lactate dehydrogenaseD I Roper, K M Moreton, D B Wigley, et al.
Journal of Molecular Biology|November 22, 1996
Guided evolution of enzymes with new substrate specificitiesA S el Hawrani, R B Sessions, K M Moreton, et al.
FEBS Letters|December 16, 1996
Removal of substrate inhibition in a lactate dehydrogenase from human muscle by a single residue changeC M Eszes, R B Sessions, A R Clarke, et al.
Trends in Biotechnology|May 1, 1994
Engineering surface loops of proteins--a preferred strategy for obtaining new enzyme functionA S el Hawrani, K M Moreton, R B Sessions, et al.
Journal of Molecular Biology|May 13, 1994
Allosteric activation in Bacillus stearothermophilus lactate dehydrogenase investigated by an X-ray crystallographic analysis of a mutant designed to prevent tetramerization of the enzymeA D Cameron, D I Roper, K M Moreton, et al.
Biochemistry|September 1, 1992
Design of a specific phenyllactate dehydrogenase by peptide loop exchange on the Bacillus stearothermophilus lactate dehydrogenase frameworkH M Wilks, K M Moreton, D J Halsall, et al.
Protein Engineering|July 2, 1999
A general method for relieving substrate inhibition in lactate dehydrogenasesC O Hewitt, C M Eszes, R B Sessions, et al.
Biochemistry|September 8, 1992
Construction of a stable dimer of Bacillus stearothermophilus lactate dehydrogenaseR M Jackson, J L Gelpi, A Cortes, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
Protein Engineering|October 1, 1992
The structural consequences of exchanging tryptophan and tyrosine residues in B. stearothermophilus lactate dehydrogenaseD I Roper, K M Moreton, D B Wigley, et al.
Journal of Molecular Biology|November 22, 1996
Guided evolution of enzymes with new substrate specificitiesA S el Hawrani, R B Sessions, K M Moreton, et al.
FEBS Letters|December 16, 1996
Removal of substrate inhibition in a lactate dehydrogenase from human muscle by a single residue changeC M Eszes, R B Sessions, A R Clarke, et al.
Trends in Biotechnology|May 1, 1994
Engineering surface loops of proteins--a preferred strategy for obtaining new enzyme functionA S el Hawrani, K M Moreton, R B Sessions, et al.
Journal of Molecular Biology|May 13, 1994
Allosteric activation in Bacillus stearothermophilus lactate dehydrogenase investigated by an X-ray crystallographic analysis of a mutant designed to prevent tetramerization of the enzymeA D Cameron, D I Roper, K M Moreton, et al.
Biochemistry|September 1, 1992
Design of a specific phenyllactate dehydrogenase by peptide loop exchange on the Bacillus stearothermophilus lactate dehydrogenase frameworkH M Wilks, K M Moreton, D J Halsall, et al.
Protein Engineering|July 2, 1999
A general method for relieving substrate inhibition in lactate dehydrogenasesC O Hewitt, C M Eszes, R B Sessions, et al.
Biochemistry|September 8, 1992
Construction of a stable dimer of Bacillus stearothermophilus lactate dehydrogenaseR M Jackson, J L Gelpi, A Cortes, et al.
Pageof 1