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Symmetric Member in Bending

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In the study of the mechanics of materials, analyzing the behavior of prismatic members under opposing couples is crucial for understanding internal stress distributions, which are essential for structural design. When subjected to couples, a prismatic member experiences internal forces that maintain equilibrium. A couple, characterized by two equal and opposite forces, creates a moment but no resultant force. The internal forces at any section cut of the member must balance these external...

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Electrocyclic reactions, cycloadditions, and sigmatropic rearrangements are concerted pericyclic reactions that proceed via a cyclic transition state. These reactions are stereospecific and regioselective. The stereochemistry of the products depends on the symmetry characteristics of the interacting orbitals and the reaction conditions. Accordingly, pericyclic reactions are classified as either symmetry-allowed or symmetry-forbidden. Woodward and Hoffmann presented the selection criteria for...

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Symmetry

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Updated: May 31, 2026

Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments

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Published on: January 20, 2022

SymmRef: a flexible refinement method for symmetric multimers.

Efrat Mashiach-Farkash¹, Ruth Nussinov, Haim J Wolfson

¹Blavatnik School of Computer Science, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Tel Aviv 69978, Israel.

|July 2, 2011

Summary

This summary is machine-generated.

SymmRef refines symmetric protein complex structures by modeling monomer movements and optimizing orientations. This novel method significantly enhances the accuracy and ranking of predicted protein complex models.

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Published on: September 26, 2016

Area of Science:

Structural biology
Computational biology
Biophysics

Background:

Symmetric protein complexes are crucial in cellular functions.
Predicting their atomic structures aids in understanding biological mechanisms.
Existing symmetric docking methods face challenges in modeling monomer conformational changes.

Purpose of the Study:

To present SymmRef, a novel method for refining and reranking symmetric protein complex docking solutions.
To address the obstacle of modeling conformational changes in monomers during symmetric docking.
To improve the accuracy and reliability of predicting the structure of symmetric protein complexes.

Main Methods:

SymmRef models backbone and side-chain movements of monomers.
Normal modes minimization is used for backbone movements.
Optimal rotamers are selected for side-chain conformations, without symmetry constraints.
Rigid-body orientations of monomers are optimized.
Refined models are reranked using an energy score.

Main Results:

SymmRef significantly improves the accuracy of symmetric rigid docking solutions.
The method enhances the ranking of predicted symmetric protein complex structures.
Tested on a benchmark of unbound docking challenges, SymmRef demonstrated improved performance.

Conclusions:

SymmRef effectively refines and reranks symmetric docking solutions.
The method successfully models conformational changes, leading to more accurate structural predictions.
SymmRef offers a valuable tool for advancing the study of symmetric protein complexes.