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Proteins2005; 60(3); 547-551; doi: 10.1002/prot.20510

A new relaxed state in horse methemoglobin characterized by crystallographic studies.

Abstract: A new relaxed state has been characterized in the crystals of horse methemoglobin grown at neutral pH at low ionic concentration and their low humidity variants. The crystals provide an example for improvement in X-ray diffraction quality with reduced solvent content. Only the classical R state has been so far observed in liganded horse hemoglobin. The state characterized in the present study lies in between the R state and the R2 state characterized earlier in liganded human hemoglobin. The results presented here, along with those of earlier studies, suggest that relaxed and tense hemoglobin can access ensembles of states.
Publication Date: 2005-05-12 PubMed ID: 15887226DOI: 10.1002/prot.20510Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The study involves the discovery of a new relaxed state in horse methemoglobin, which was identified through crystallographic studies. The research highlights the potential existence of multiple states in relaxed and tense hemoglobin.

Introduction to the Research

  • The research aimed to explore the relaxed states of horse methemoglobin through crystallographic studies at a neutral pH and low ionic concentration.
  • The researchers used crystals of horse methemoglobin under low humidity variants to conduct their study.
  • The new state was discovered in-between the R (relaxed) state and R2 state previously identified in liganded human hemoglobin.

Research Methodology

  • The study was performed by growing crystals of horse methemoglobin at neutral pH at low ionic concentration. These conditions allowed for the exploration of different states of the hemoglobin.
  • The low humidity variants of the methemoglobin crystals were used for the examination, providing an improved example of X-ray diffraction with lesser solvent content.
  • The research also included careful comparisons with the previously identified states in liganded human hemoglobin.

Research Findings

  • A new, previously uncharacterized relaxed state was discovered in the horse methemoglobin crystals. This new state was found to lie between the classically recognized R state and previously characterized R2 state in human hemoglobin.
  • These findings suggest the possibility of various accessible states in both relaxed and tense versions of hemoglobin, potentially setting the stage for further studies in hemoglobin states.

Significance of Research

  • The significance of this research lies in the discovery of the new relaxed state in the horse methemoglobin crystals, which deepens the scientific understanding of hemoglobin in its different states.
  • The findings also propose that hemoglobin in both its relaxed and tense states can access multiple states, which could lead to new approaches in medical and health-related investigations involving hemoglobin.

Cite This Article

APA
Sankaranarayanan R, Biswal BK, Vijayan M. (2005). A new relaxed state in horse methemoglobin characterized by crystallographic studies. Proteins, 60(3), 547-551. https://doi.org/10.1002/prot.20510

Publication

ISSN: 1097-0134
NlmUniqueID: 8700181
Country: United States
Language: English
Volume: 60
Issue: 3
Pages: 547-551

Researcher Affiliations

Sankaranarayanan, R
  • Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Biswal, B K
    Vijayan, M

      MeSH Terms

      • Animals
      • Carboxyhemoglobin / chemistry
      • Crystallography, X-Ray / methods
      • Hemoglobins / chemistry
      • Horses
      • Humans
      • Hydrogen-Ion Concentration
      • Ions
      • Methemoglobin / chemistry
      • Models, Molecular
      • Protein Conformation
      • Protein Structure, Quaternary
      • Protein Structure, Tertiary
      • Solvents
      • X-Ray Diffraction

      Citations

      This article has been cited 3 times.
      1. Smart OS, Womack TO, Flensburg C, Keller P, Paciorek W, Sharff A, Vonrhein C, Bricogne G. Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER. Acta Crystallogr D Biol Crystallogr 2012 Apr;68(Pt 4):368-80.
        doi: 10.1107/S0907444911056058pubmed: 22505257google scholar: lookup
      2. Kaushal PS, Sankaranarayanan R, Vijayan M. Water-mediated variability in the structure of relaxed-state haemoglobin. Acta Crystallogr Sect F Struct Biol Cryst Commun 2008 Jun 1;64(Pt 6):463-9.
        doi: 10.1107/S1744309108013109pubmed: 18540052google scholar: lookup
      3. Valenci Y, Tobi D. Exploring the Hemoglobin T to R2 Path Using Gaussian Elastic Network Correlation Map Distance. Proteins 2025 Dec;93(12):2128-2137.
        doi: 10.1002/prot.70014pubmed: 40616438google scholar: lookup