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

Solution NMR studies of intact lambda repressor.

M A Weiss1, M Karplus, D J Patel

  • 1Department of Chemistry, Harvard University, Cambridge MA 02138.

Journal of Biomolecular Structure & Dynamics
|October 1, 1983
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

Hemodynamics.

Annual review of physiology·2009
Same author

Structural biology of RNA silencing and its functional implications.

Cold Spring Harbor symposia on quantitative biology·2007
Same author

1H-1H correlations across N-H...N hydrogen bonds in nucleic acids.

Journal of biomolecular NMR·2002
Same author

Cyclohexene ring and Fjord region twist inversion in stereoisomeric DNA adducts of enantiomeric benzo[c]phenanthrene diol epoxides.

Chemical research in toxicology·2001
Same author

Additional hydrogen bonds and base-pair kinetics in the symmetrical AMP-DNA aptamer complex.

Biophysical journal·2001
Same author

Why is recurrent myocardial ischaemia a predictor of adverse outcome in unstable angina? An observational study of myocardial ischaemia and its relation to coronary anatomy.

European heart journal·2001
Same journal

Anti-mycobacterial activity of phytocompounds from <i>Ricinus communis</i> L. - an integrated <i>in-vitro</i> and <i>in-silico</i> approach.

Journal of biomolecular structure & dynamics·2026
Same journal

Binding studies of the X-ray characterized [SnMe<sub>2</sub>Cl<sub>2</sub>(Me<sub>2</sub>phen)] complex with human serum albumin: experimental and molecular docking approaches.

Journal of biomolecular structure & dynamics·2026
Same journal

Computational design and experimental validation of peptide inhibitors to disrupt urease enzyme maturation in pathogenic bacteria <i>Proteus mirabilis</i>.

Journal of biomolecular structure & dynamics·2026
Same journal

Wavelet-domain multiway spectral separation of free drug, DNA, and drug-DNA complex profiles for quantitative binding analysis based on fractional occupancy (<i>θ</i>).

Journal of biomolecular structure & dynamics·2026
Same journal

Gene expression and microsecond scale conformational dynamics suggest potential regulatory mechanisms for the expanded subtilase family of <i>T. rubrum</i>.

Journal of biomolecular structure & dynamics·2026
Same journal

Deciphering the Role of Sugar Osmolytes in Free and Nano forms to Mitigate Protein Aggregation: Insights from Biophysical and Microscopic Studies.

Journal of biomolecular structure & dynamics·2026
See all related articles

The N-terminal domain of bacteriophage lambda repressor maintains its structure within the intact protein. This domain is only loosely associated with the C-terminal domain, as revealed by NMR spectroscopy.

Area of Science:

  • Molecular biology
  • Structural biology
  • Biophysics

Background:

  • Bacteriophage lambda repressor is a key protein in viral DNA replication.
  • Understanding the structural dynamics of lambda repressor is crucial for its biological function.

Purpose of the Study:

  • To determine the structural conformation of the N-terminal domain within the intact bacteriophage lambda repressor.
  • To investigate the interaction between the N-terminal and C-terminal domains of the repressor.

Main Methods:

  • Two-dimensional Nuclear Magnetic Resonance (2D NMR) spectroscopy.
  • One-dimensional Nuclear Magnetic Resonance (1D NMR) spectroscopy.

Main Results:

  • The N-terminal domain retains its native global structure when part of the intact bacteriophage lambda repressor.

Related Experiment Videos

  • The N-terminal domain exhibits a loose association with the C-terminal domain in the intact repressor.

    • Conclusions:

    • The structural integrity of the N-terminal domain is maintained regardless of its association with the C-terminal domain.
    • The findings suggest a flexible interaction between the repressor's domains, potentially allowing for regulatory conformational changes.