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

Protein-ligand binding with a missing species.

W E Briggs1

  • 1Department of Mathematics, University of Colorado, Boulder 80309.

Journal of Theoretical Biology
|August 22, 1988
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

Analysis of zeros of binding polynomials for tetrameric hemoglobins.

Biophysical chemistry·1986
Same author

A probabilistic model for fitting MWC polynomials in protein-ligand binding.

Biophysical chemistry·1986
Same author

The relationship between zeros and factors of binding polynomials and cooperativity in protein-ligand binding.

Journal of theoretical biology·1985
Same author

Cooperativity and extrema of the Hill slope for symmetric protein-ligand binding polynomials.

Journal of theoretical biology·1984
Same author

A new measure of cooperativity in protein-ligand binding.

Biophysical chemistry·1983
Same author

Improving productivity in the x-ray film file room.

Applied radiology·1983

The binding of oxygen to tetrameric hemoglobins rarely involves a triply-ligated state. Mathematical analysis of the binding polynomial shows this near-zero intermediate affects hemoglobin

Area of Science:

  • Biochemistry
  • Biophysics
  • Physical Chemistry

Background:

  • Tetrameric hemoglobins exhibit complex oxygen and carbon monoxide binding.
  • Experimental data suggests a near-absence of triply-ligated hemoglobin species.
  • The binding polynomial mathematically models ligand-protein interactions.

Purpose of the Study:

  • To investigate the mathematical properties of binding polynomials when the triply-ligated species is negligible (beta n-1 ≈ 0).
  • To analyze the impact of a near-zero beta n-1 on hemoglobin binding characteristics.
  • To compare theoretical predictions with experimental data from tetrameric hemoglobins.

Main Methods:

  • Mathematical analysis of binding polynomial zeros and factorization for the general case (beta n-1 = 0).

Related Experiment Videos

  • Detailed analysis for n=3 and n=4 binding polynomials.
  • Comparison of theoretical binding polynomial properties with experimental data from various tetrameric hemoglobins.

    • Main Results:

    • The binding polynomial P(x) = 1 + beta 1x + ... + beta nxn simplifies when beta n-1 is nearly zero.
    • Analysis reveals how zeros, factorization, and Hill plots are affected by beta n-1 ≈ 0.
    • Experimental data for hemoglobins with small beta 3 aligns with theoretical predictions.

    Conclusions:

    • A near-zero triply-ligated species (small beta 3) has minimal impact on most binding properties.
    • Key affected properties include fractional saturation, maximum Hill slope, and binding polynomial factorization.
    • The high-saturation asymptote slope of the Hill plot is notably influenced by the beta n-1 term.