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

R Nagaraj

Showing results (1-10 of 120) with videos related to

Pageof 12
Sort By:
Journal of Biomolecular Structure & Dynamics|December 15, 2010
Is protein folding still a challenge?R Nagaraj
FEBS Letters|January 2, 1984
Interaction of synthetic signal sequence fragments with model membranesR Nagaraj
Journal of Biomolecular Structure & Dynamics|January 10, 2013
Is Levinthal's question answered after a revisit?R Nagaraj
The Journal of Peptide Research : Official Journal of the American Peptide Society|August 1, 1997
Antimicrobial and hemolytic activities of crabrolin, a 13-residue peptide from the venom of the European hornet, Vespa crabro, and its analogsV Krishnakumari, R Nagaraj
Biochemistry|May 12, 1981
Conformations of synthetic alamethicin fragments. Evidence for 310 helical folding from 270-MHz hydrogen-1 nuclear magnetic resonance and circular dichroism studiesR Nagaraj, P Balaram
The Journal of Biological Chemistry|August 18, 1995
Conformations of peptides corresponding to fatty acylation sites in proteins. A circular dichroism studyM Joseph, R Nagaraj
The Journal of Biological Chemistry|July 5, 1993
Conformations of peptide fragments comprising the amino-terminal, central, and carboxyl-terminal regions of a membrane-active polypeptide. Build-up of secondary structure in pardaxinG Saberwal, R Nagaraj
Biochemistry|March 30, 1993
Interaction of the 47-residue antibacterial peptide seminalplasmin and its 13-residue fragment which has antibacterial and hemolytic activities with model membranesN Sitaram, R Nagaraj
Biochimica Et Biophysica Acta|September 5, 1993
Interaction of hydrophobic peptides with model membranes: slow binding to membranes and not subtle variations in pore structure is responsible for the gradual release of entrapped solutesG Saberwal, R Nagaraj
Indian Journal of Biochemistry & Biophysics|October 1, 1996
Acylation of proteins: recent advancesM Joseph, R Nagaraj
Pageof 12

Showing results (1-10 of 120) with videos related to

Sort By:
Pageof 12
Journal of Biomolecular Structure & Dynamics|December 15, 2010
Is protein folding still a challenge?R Nagaraj
FEBS Letters|January 2, 1984
Interaction of synthetic signal sequence fragments with model membranesR Nagaraj
Journal of Biomolecular Structure & Dynamics|January 10, 2013
Is Levinthal's question answered after a revisit?R Nagaraj
The Journal of Peptide Research : Official Journal of the American Peptide Society|August 1, 1997
Antimicrobial and hemolytic activities of crabrolin, a 13-residue peptide from the venom of the European hornet, Vespa crabro, and its analogsV Krishnakumari, R Nagaraj
Biochemistry|May 12, 1981
Conformations of synthetic alamethicin fragments. Evidence for 310 helical folding from 270-MHz hydrogen-1 nuclear magnetic resonance and circular dichroism studiesR Nagaraj, P Balaram
The Journal of Biological Chemistry|August 18, 1995
Conformations of peptides corresponding to fatty acylation sites in proteins. A circular dichroism studyM Joseph, R Nagaraj
The Journal of Biological Chemistry|July 5, 1993
Conformations of peptide fragments comprising the amino-terminal, central, and carboxyl-terminal regions of a membrane-active polypeptide. Build-up of secondary structure in pardaxinG Saberwal, R Nagaraj
Biochemistry|March 30, 1993
Interaction of the 47-residue antibacterial peptide seminalplasmin and its 13-residue fragment which has antibacterial and hemolytic activities with model membranesN Sitaram, R Nagaraj
Biochimica Et Biophysica Acta|September 5, 1993
Interaction of hydrophobic peptides with model membranes: slow binding to membranes and not subtle variations in pore structure is responsible for the gradual release of entrapped solutesG Saberwal, R Nagaraj
Indian Journal of Biochemistry & Biophysics|October 1, 1996
Acylation of proteins: recent advancesM Joseph, R Nagaraj
Pageof 12