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

Modeling of alpha-MSH conformations with implicit solvent.

N V Prabhu1, J S Perkyns, B M Pettitt

  • 1Department of Chemistry, University of Houston, TX 77204-5641, USA.

The Journal of Peptide Research : Official Journal of the American Peptide Society
|November 24, 1999
PubMed
Summary

Researchers modeled alpha-melanocyte-stimulating hormone (alpha-MSH) structures in water to understand its biological activity. The minimum energy structure revealed a stable beta-turn, suggesting key features for receptor interaction.

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

Correction: Study on the inflammatory response of PMMA/polystyrene/silica nanocomposite membranes for drug delivery and dental applications.

PloS one·2019
Same author

The contribution of electrostatic interactions to the collapse of oligoglycine in water.

Condensed matter physics·2017
Same author

The theoretical basis of universal identification systems for bacteria and viruses.

Journal of biological physics and chemistry : JBPC·2010
Same author

Fast multipole methods for particle dynamics.

Molecular simulation·2009
Same author

Systematic investigation of theories of transport in the Lennard-Jones fluid.

The Journal of chemical physics·2007
Same author

Simple bond length dependence: a correspondence between reactive fluid theories.

The Journal of chemical physics·2005

Area of Science:

  • Biochemistry
  • Computational Chemistry
  • Molecular Biology

Background:

  • Alpha-melanocyte-stimulating hormone (alpha-MSH) is a peptide hormone crucial for various physiological processes.
  • Understanding the conformational dynamics of alpha-MSH is essential for elucidating its biological activity and receptor interactions.

Purpose of the Study:

  • To determine the structural features of alpha-MSH essential for its biological activity by performing a conformational search in aqueous solution.
  • To model the free-energy surface of alpha-MSH and identify low-energy conformations.

Main Methods:

  • Utilized integral equation theory to model the free-energy surface of alpha-MSH.
  • Employed high-temperature molecular dynamics to enhance conformational sampling.
  • Performed a conformational search to identify probable structures in aqueous solution.

Related Experiment Videos

Main Results:

  • Identified families of low free-energy structures for alpha-MSH.
  • The minimum energy structure exhibited a stable beta-turn in the message region, stabilized by a Glu5-Lys11 salt bridge.
  • Observed specific side-chain interactions, including hydrophobic contacts (His6, Phe7, Trp9) and an amphiphilic orientation, aligning with experimental data.

Conclusions:

  • The identified structural features of alpha-MSH are critical for its biological function.
  • Proposed a receptor-hormone interaction model where hydrophobic residues (Phe7, Trp9) interact with the transmembrane domain of the human melanocortin 1 (MC1) receptor.
  • Suggested potential interactions of charged/polar residues (Arg8, His6) with extracellular loops of the MC1 receptor.