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Updated: May 22, 2026

Analyzing Tumor Gene Expression Factors with the CorExplorer Web Portal
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Published on: October 11, 2019

MaxOcc: a web portal for maximum occurrence analysis.

Ivano Bertini1, Lucio Ferella, Claudio Luchinat

  • 1Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, FI, Italy. ivanobertini@cerm.unifi.it

Journal of Biomolecular NMR
|May 29, 2012
PubMed
Summary
This summary is machine-generated.

The MaxOcc web portal characterizes protein conformational heterogeneity by calculating Maximum Occurrence values for each conformation using experimental data. This tool helps understand protein dynamics and structural flexibility.

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Last Updated: May 22, 2026

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05:01

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Published on: July 1, 2020

Area of Science:

  • Structural Biology
  • Computational Biology
  • Biophysics

Background:

  • Proteins often exist as an ensemble of different conformations.
  • Characterizing this conformational heterogeneity is crucial for understanding protein function.
  • Existing methods may not fully capture the dynamic nature of protein structures.

Purpose of the Study:

  • To present the MaxOcc web portal for characterizing protein conformational heterogeneity.
  • To enable the calculation of Maximum Occurrence values for protein conformations.
  • To provide a tool that integrates various experimental data types for structural analysis.

Main Methods:

  • The MaxOcc portal calculates the Maximum Occurrence for protein conformations.
  • It utilizes experimental data including pseudocontact shifts, residual dipolar couplings, and small angle X-ray scattering.
  • Input requires the 3D structure of the two-domain protein.

Main Results:

  • MaxOcc provides a quantitative measure (Maximum Occurrence) for the plausibility of protein conformations.
  • The calculated Maximum Occurrence sets an upper limit on the population of any given conformation.
  • The portal integrates multiple experimental restraints for robust characterization.

Conclusions:

  • MaxOcc offers a novel approach to quantify conformational heterogeneity in proteins.
  • The web portal facilitates the analysis of protein dynamics using diverse experimental data.
  • This tool enhances the characterization of two-domain protein structures and their flexibility.