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 W Matthews

Showing results (41-50 of 229) with videos related to

Pageof 23
Sort By:
Biochimica Et Biophysica Acta|March 10, 2000
Structure and function of the methionine aminopeptidasesW T Lowther, B W Matthews
Protein Engineering|March 1, 1994
Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linkingD W Heinz, B W Matthews
Current Opinion in Biotechnology|August 1, 1994
Core-packing constraints, hydrophobicity and protein designE P Baldwin, B W Matthews
Journal of Molecular Biology|August 28, 1971
Symmetry, molecular weight and crystallographic data for sweet potato -amylaseP M Colman, B W Matthews
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1978
A general method to assess similarity of protein structures, with applications to T4 bacteriophage lysozymeS J Remington, B W Matthews
Protein Science : a Publication of the Protein Society|August 22, 2001
A structural basis for processivityW A Breyer, B W Matthews
The Journal of Biological Chemistry|August 10, 1977
Crystallographic data for chicken liver fructose bisphosphataseW F Anderson, B W Matthews
Nature|November 15, 1990
A mutant T4 lysozyme displays five different crystal conformationsH R Faber, B W Matthews
Biochemistry|May 31, 1977
Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysisW R Kester, B W Matthews
Journal of Molecular Biology|January 25, 1982
Amino acid substitutions far from the active site of bacteriophage T4 lysozyme reduce catalytic activity and suggest that the C-terminal lobe of the enzyme participates in substrate bindingM G Grütter, B W Matthews
Pageof 23

Showing results (41-50 of 229) with videos related to

Sort By:
Pageof 23
Biochimica Et Biophysica Acta|March 10, 2000
Structure and function of the methionine aminopeptidasesW T Lowther, B W Matthews
Protein Engineering|March 1, 1994
Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linkingD W Heinz, B W Matthews
Current Opinion in Biotechnology|August 1, 1994
Core-packing constraints, hydrophobicity and protein designE P Baldwin, B W Matthews
Journal of Molecular Biology|August 28, 1971
Symmetry, molecular weight and crystallographic data for sweet potato -amylaseP M Colman, B W Matthews
Proceedings of the National Academy of Sciences of the United States of America|May 1, 1978
A general method to assess similarity of protein structures, with applications to T4 bacteriophage lysozymeS J Remington, B W Matthews
Protein Science : a Publication of the Protein Society|August 22, 2001
A structural basis for processivityW A Breyer, B W Matthews
The Journal of Biological Chemistry|August 10, 1977
Crystallographic data for chicken liver fructose bisphosphataseW F Anderson, B W Matthews
Nature|November 15, 1990
A mutant T4 lysozyme displays five different crystal conformationsH R Faber, B W Matthews
Biochemistry|May 31, 1977
Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysisW R Kester, B W Matthews
Journal of Molecular Biology|January 25, 1982
Amino acid substitutions far from the active site of bacteriophage T4 lysozyme reduce catalytic activity and suggest that the C-terminal lobe of the enzyme participates in substrate bindingM G Grütter, B W Matthews
Pageof 23