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

Related Experiment Videos

Nuclear magnetic resonance studies on complementary peptides

E V Curto1, N R Krishna

  • 1Department of Biochemistry and Molecular Genetics, University of Alabama, Birmingham 35294.

Immunomethods
|October 1, 1994
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Solution structure of an insect-specific neurotoxin from the New World scorpion Centruroides sculpturatus Ewing.

Biochemistry·2001
Same author

An economical method for (15)N/(13)C isotopic labeling of proteins expressed in Pichia pastoris.

Journal of biochemistry·2001
Same author

Solution NMR structure of a model class A (apolipoprotein) amphipathic alpha helical peptide.

Peptides·2001
Same author

Automatic assignment of NOESY cross peaks and determination of the protein structure of a new world scorpion neurotoxin using NOAH/DIAMOD.

Journal of magnetic resonance (San Diego, Calif. : 1997)·2001
Same author

Molecular structure of the carbohydrate-protein linkage region fragments from connective-tissue proteoglycans.

Advances in carbohydrate chemistry and biochemistry·2000
Same author

Expression of functional recombinant scorpion beta-neurotoxin Css II in E. coli.

Peptides·2000

Complementary peptides, based on molecular recognition theory, form complexes with inverted hydropathic profiles. This review focuses on solution Nuclear Magnetic Resonance (NMR) studies to understand these peptide interactions.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Molecular recognition theory explains interactions between complementary peptides based on DNA codon complementarity.
  • Peptides with inverted hydropathic profiles are known to form complexes in various assays.
  • Understanding the molecular forces driving these peptide complexes is limited.

Purpose of the Study:

  • To review solution Nuclear Magnetic Resonance (NMR) studies on complementary peptide interactions.
  • To provide insights into the three-dimensional structures of complexes formed by interacting complementary peptides.

Main Methods:

  • Review of published solution NMR spectroscopy data from multiple research groups.
  • Analysis of structural data to elucidate peptide-peptide interactions.

Related Experiment Videos

Main Results:

  • NMR studies have been employed to investigate the structural basis of complementary peptide complex formation.
  • These studies aim to map the interactions and determine the three-dimensional structures of the complexes.

Conclusions:

  • Solution NMR is a valuable technique for studying complementary peptide interactions.
  • Further structural elucidation is needed to fully understand the molecular forces involved in these complexes.