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

Myoglobin solvent structure at different temperatures

B V Daniels1, B P Schoenborn, Z R Korszun

  • 1Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA.

Basic Life Sciences
|January 1, 1996
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

The use of complementary and alternative medicine by women transitioning through menopause in Germany: results of a survey of women aged 45-60 years.

Complementary therapies in medicine·2014
Same author

A preliminary time-of-flight neutron diffraction study on amicyanin from Paracoccus denitrificans.

Acta crystallographica. Section D, Biological crystallography·2005
Same author

A low-resolution low-temperature neutron diffraction study of myoglobin.

Acta crystallographica. Section D, Biological crystallography·2004
Same author

Enhanced visibility of hydrogen atoms by neutron crystallography on fully deuterated myoglobin.

Proceedings of the National Academy of Sciences of the United States of America·2000
Same author

Need for neutron diffraction instruments.

Science (New York, N.Y.)·1999
Same author

Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine.

Structure (London, England : 1993)·1998
Same journal

Catechin and procyanidin levels in French wines: contribution to dietary intake.

Basic life sciences·2000
Same journal

Proceedings of the 3rd Tannin Conference. In honor of Professor Edwin Haslam. Bend, Oregon, USA. July 20-25, 1998.

Basic life sciences·2000
Same journal

Tannins as nutritional constraints for elk and deer of the coastal Pacific Northwest.

Basic life sciences·2000
Same journal

Phenolic content and antioxidant activity: a study on plants eaten by a group of howler monkeys (Alouatta fusca).

Basic life sciences·2000
Same journal

Modification of the solubility of tannins: biological significance and synthesis of lipid-soluble polyphenols.

Basic life sciences·2000
Same journal

Functional properties of hop polyphenols.

Basic life sciences·2000
See all related articles

Neutron diffraction reveals that water molecules around myoglobin crystals form distinct hydration shells, not disordered solvent. These ordered shells expand with increasing temperature, indicating a phase transition around 180K.

Area of Science:

  • Biophysics
  • Structural Biology
  • Crystallography

Background:

  • Understanding protein hydration is crucial for biological function.
  • Previous studies suggested disordered solvent around protein crystals.
  • Myoglobin serves as a model protein for studying hydration dynamics.

Purpose of the Study:

  • To investigate the structural organization of water molecules surrounding myoglobin crystals.
  • To determine if the solvent exhibits ordered hydration shells or disordered structure.
  • To analyze the effect of temperature on protein hydration structure.

Main Methods:

  • Neutron diffraction data collection at multiple temperatures (80K, 130K, 180K, 240K).
  • Analysis of low-resolution data using Relative Wilson Statistics.

Related Experiment Videos

  • Quantification of solvent structure using the liquidity factor (Bsn) as a function of distance from the protein surface.
  • Main Results:

    • Evidence of a phase transition in the solvent structure around 180K.
    • Identification of two distinct, well-defined hydration shells surrounding the myoglobin crystals.
    • Observation that both hydration shells expand with increasing temperature.
    • The liquidity factor (Bsn) shows minima at approximately 2.35Å and 3.85Å from the protein surface.

    Conclusions:

    • The solvent structure around myoglobin crystals is not disordered but organized into specific hydration shells.
    • Temperature significantly influences the expansion and structure of these hydration shells.
    • A phase transition occurs around 180K, affecting the solvent's structural organization.