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Updated: Jan 28, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
Minimal NMR distance information for rigidity of protein graphs
Carlile Lavor1, Leo Liberti2, Bruce Donald3
1University of Campinas (IMECC-UNICAMP), 13081-970, Campinas - SP, Brazil.
Abstract:
Nuclear Magnetic Resonance (NMR) experiments provide distances between nearby atoms of a protein molecule. The corresponding structure determination problem is to determine the 3D protein structure by exploiting such distances. We present a new order on the atoms of the protein, based on information from the chemistry of proteins and NMR experiments, which allows us to formulate the problem as a combinatorial search. Additionally, this order tells us what kind of NMR distance information is crucial to understand the cardinality of the solution set of the problem and its computational complexity.
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