Looking for central tendencies in the conformational freedom of proteins using NMR measurements

TL;DR

This paper introduces a new algorithm to determine the central tendency of a protein's conformational distribution using NMR measurements, enhancing understanding of protein flexibility.

Contribution

The paper presents a novel algorithm for calculating the Maximum Allowable Probability, applicable to various NMR measurements, to identify central tendencies in protein conformations.

Findings

Reconstructed a single central tendency in the conformational distribution

Applied the method to Pseudo Contact Shifts and Residual Dipolar Coupling data

Discussed implications for protein flexibility analysis

Abstract

We study the conformational freedom of a protein made by two rigid domains connected by a flexible linker. The conformational freedom is represented as an unknown probability distribution on the space of allowed states. A new algorithm for the calculation of the Maximum Allowable Probability is proposed, which can be extended to any type of measurements. In this paper we use Pseudo Contact Shifts and Residual Dipolar Coupling. We reconstruct a single central tendency in the distribution and discuss in depth the results.