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

T M Lohman

Showing results (21-30 of 87) with videos related to

Pageof 9
Sort By:
Methods in Enzymology|January 1, 1991
Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor bindingT M Lohman, W Bujalowski
The Journal of Biological Chemistry|January 15, 1990
DNA and nucleotide-induced conformational changes in the Escherichia coli Rep and helicase II (UvrD) proteinsK Chao, T M Lohman
Biochemistry|December 2, 1986
Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNAW Bujalowski, T M Lohman
Journal of Molecular Biology|May 5, 1989
Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. II. Salt, temperature and oligonucleotide length effectsW Bujalowski, T M Lohman
Journal of Molecular Biology|June 20, 1998
Calorimetric studies of E. coli SSB protein-single-stranded DNA interactions. Effects of monovalent salts on binding enthalpyA G Kozlov, T M Lohman
Biochemistry|June 3, 1999
Adenine base unstacking dominates the observed enthalpy and heat capacity changes for the Escherichia coli SSB tetramer binding to single-stranded oligoadenylatesA G Kozlov, T M Lohman
Science (New York, N.Y.)|January 17, 1997
Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicaseJ A Ali, T M Lohman
Journal of Molecular Biology|February 11, 1994
Linkage of pH, anion and cation effects in protein-nucleic acid equilibria. Escherichia coli SSB protein-single stranded nucleic acid interactionsL B Overman, T M Lohman
Proceedings of the National Academy of Sciences of the United States of America|April 1, 1990
Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acidsD P Mascotti, T M Lohman
Biochemistry|December 6, 1994
Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 2. Application of a kinetic competition approachK J Moore, T M Lohman
Pageof 9

Showing results (21-30 of 87) with videos related to

Sort By:
Pageof 9
Methods in Enzymology|January 1, 1991
Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor bindingT M Lohman, W Bujalowski
The Journal of Biological Chemistry|January 15, 1990
DNA and nucleotide-induced conformational changes in the Escherichia coli Rep and helicase II (UvrD) proteinsK Chao, T M Lohman
Biochemistry|December 2, 1986
Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNAW Bujalowski, T M Lohman
Journal of Molecular Biology|May 5, 1989
Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. II. Salt, temperature and oligonucleotide length effectsW Bujalowski, T M Lohman
Journal of Molecular Biology|June 20, 1998
Calorimetric studies of E. coli SSB protein-single-stranded DNA interactions. Effects of monovalent salts on binding enthalpyA G Kozlov, T M Lohman
Biochemistry|June 3, 1999
Adenine base unstacking dominates the observed enthalpy and heat capacity changes for the Escherichia coli SSB tetramer binding to single-stranded oligoadenylatesA G Kozlov, T M Lohman
Science (New York, N.Y.)|January 17, 1997
Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicaseJ A Ali, T M Lohman
Journal of Molecular Biology|February 11, 1994
Linkage of pH, anion and cation effects in protein-nucleic acid equilibria. Escherichia coli SSB protein-single stranded nucleic acid interactionsL B Overman, T M Lohman
Proceedings of the National Academy of Sciences of the United States of America|April 1, 1990
Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acidsD P Mascotti, T M Lohman
Biochemistry|December 6, 1994
Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 2. Application of a kinetic competition approachK J Moore, T M Lohman
Pageof 9