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

C R Matthews

Showing results (61-70 of 82) with videos related to

Pageof 9
Sort By:
Biochemistry|March 15, 1983
Effect of a single amino acid substitution on the folding of the alpha subunit of tryptophan synthaseC R Matthews, M M Crisanti, J T Manz, et al.
Biochemistry|February 13, 1990
Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reactionN B Tweedy, M R Hurle, B A Chrunyk, et al.
The Journal of Biological Chemistry|September 25, 1975
Nuclear magnetic resonance titration curves of histidine ring protons. The effect of temperature on ribonuclease AD G Westmoreland, C R Matthews, M B Hayes, et al.
Biochemistry|April 9, 1999
Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation timeO Bilsel, L Yang, J A Zitzewitz, et al.
Biophysical Journal|March 20, 2020
Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1Noah R Cohen, Can Kayatekin, Jill A Zitzewitz, et al.
Biochemistry|October 3, 1995
Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopyJ A Zitzewitz, O Bilsel, J Luo, et al.
Biochemistry|August 6, 1991
Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopyK Kuwajima, E P Garvey, B E Finn, et al.
Biochemistry|September 19, 1989
Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductaseK M Perry, J J Onuffer, M S Gittelman, et al.
Biochemistry|October 3, 1995
Characterization of the tryptophan binding site of Escherichia coli tryptophan holorepressor by phosphorescence and optical detection of magnetic resonance of a tryptophan-free mutantZ Li, A H Maki, M R Eftink, et al.
Cold Spring Harbor Symposia on Quantitative Biology|January 1, 1987
The role of protein folding in the evolution of protein sequencesT Stackhouse, J J Onuffer, C R Matthews, et al.
Pageof 9

Showing results (61-70 of 82) with videos related to

Sort By:
Pageof 9
Biochemistry|March 15, 1983
Effect of a single amino acid substitution on the folding of the alpha subunit of tryptophan synthaseC R Matthews, M M Crisanti, J T Manz, et al.
Biochemistry|February 13, 1990
Multiple replacements at position 211 in the alpha subunit of tryptophan synthase as a probe of the folding unit association reactionN B Tweedy, M R Hurle, B A Chrunyk, et al.
The Journal of Biological Chemistry|September 25, 1975
Nuclear magnetic resonance titration curves of histidine ring protons. The effect of temperature on ribonuclease AD G Westmoreland, C R Matthews, M B Hayes, et al.
Biochemistry|April 9, 1999
Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation timeO Bilsel, L Yang, J A Zitzewitz, et al.
Biophysical Journal|March 20, 2020
Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1Noah R Cohen, Can Kayatekin, Jill A Zitzewitz, et al.
Biochemistry|October 3, 1995
Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopyJ A Zitzewitz, O Bilsel, J Luo, et al.
Biochemistry|August 6, 1991
Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopyK Kuwajima, E P Garvey, B E Finn, et al.
Biochemistry|September 19, 1989
Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductaseK M Perry, J J Onuffer, M S Gittelman, et al.
Biochemistry|October 3, 1995
Characterization of the tryptophan binding site of Escherichia coli tryptophan holorepressor by phosphorescence and optical detection of magnetic resonance of a tryptophan-free mutantZ Li, A H Maki, M R Eftink, et al.
Cold Spring Harbor Symposia on Quantitative Biology|January 1, 1987
The role of protein folding in the evolution of protein sequencesT Stackhouse, J J Onuffer, C R Matthews, et al.
Pageof 9