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

Relaxations and fluctuations in myoglobin.

H Frauenfelder1, B H McMahon

  • 1Center for Nonlinear Studies, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. frauenfelder@lanl.gov

Bio Systems
|October 12, 2001
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

Coupling Vector-host Dynamics with Weather Geography and Mitigation Measures to Model Rift Valley Fever in Africa.

Mathematical modelling of natural phenomena·2015
Same author

The association between cervical spine curvature and neck pain.

European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society·2006
Same author

Protein folding is slaved to solvent motions.

Proceedings of the National Academy of Sciences of the United States of America·2006
Same author

Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glasses, control protein motions and functions.

Proceedings of the National Academy of Sciences of the United States of America·2004
Same author

Myoglobin: the hydrogen atom of biology and a paradigm of complexity.

Proceedings of the National Academy of Sciences of the United States of America·2003
Same author

Slaving: solvent fluctuations dominate protein dynamics and functions.

Proceedings of the National Academy of Sciences of the United States of America·2002

Researchers are exploring myoglobin (Mb) as a model protein to understand biomolecular principles. Decades of research on Mb

Area of Science:

  • Biological Physics
  • Protein Science
  • Biomolecular Dynamics

Background:

  • Proteins are fundamental biomolecules governed by specific physical concepts and laws.
  • Studying a model protein is crucial due to the vast diversity of proteins (over 10^5).
  • Myoglobin (Mb) has served as a valuable prototype for protein research.

Purpose of the Study:

  • To review the progress in understanding myoglobin over the past 50+ years.
  • To highlight the potential of myoglobin as a model system for connecting protein properties.
  • To explore the relationship between protein structure, dynamics, and function.

Main Methods:

  • Literature review of 50+ years of myoglobin research.
  • Analysis of experimental and theoretical studies on myoglobin.

Related Experiment Videos

  • Synthesis of findings to connect various aspects of protein behavior.

    • Main Results:

    • Myoglobin exhibits sufficient simplicity for detailed study yet complexity to represent biomolecular characteristics.
    • Significant progress has been made in understanding myoglobin's properties.
    • The study of myoglobin offers insights into the interplay of structure, kinetics, energy landscape, dynamics, and function.

    Conclusions:

    • Myoglobin serves as an excellent model for deciphering fundamental biomolecular principles.
    • Connecting protein structure, kinetics, energy landscape, dynamics, and function remains a key goal.
    • Continued research on myoglobin provides hope for achieving a comprehensive understanding of protein behavior.