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Related Concept Videos

Chair Conformation of Cyclohexane02:02

Chair Conformation of Cyclohexane

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The chair conformation is the most stable form of cyclohexane due to the absence of angle and torsional strain. The absence of angle strain is a result of cyclohexane’s bond angle being very close to the ideal tetrahedral bond angle of 109.5° in its chair conformer. Similarly, the torsional strain is also absent owing to the perfectly staggered arrangement of bonds.
The hydrogen atoms linked to carbons are arranged in two different axial and equatorial orientations to achieve this...
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Stability of structures01:14

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In mechanical engineering, the stability of systems under various forces is critical for designing durable and efficient structures. One fundamental way to explore these concepts is by analyzing systems like two rods connected at a pivot point, O, with a torsional spring of spring constant k at the pivot point. This system is similar in appearance to a scissor jack used to change tires on a car. In this case, the arms of the linkage (equivalent to the rods in this system) are entirely vertical,...
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Overview
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Stability of Substituted Cyclohexanes02:30

Stability of Substituted Cyclohexanes

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This lesson discusses the stability of substituted cyclohexanes with a focus on energies of various conformers and the effect of 1,3-diaxial interactions.
The two chair conformations of cyclohexanes undergo rapid interconversion at room temperature. Both forms have identical energies and stabilities, each comprising equal amounts of the equilibrium mixture. Replacing a hydrogen atom with a functional group makes the two conformations energetically non-equivalent.
For example, in...
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Symmetric Member in Bending01:07

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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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Conformations of Cyclohexane02:11

Conformations of Cyclohexane

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Cyclohexane does not exist in a planar form due to the high angle and torsional strain it would experience in the planar structure. Instead, it adopts non-planar chair and boat conformations.
The chair form is the most stable and derives its name from its resemblance to the “easy chair.” In the chair conformation, two carbon atoms are arranged out-of-plane — one above and one below, minimizing the torsional strain. In the chair form, the bond angle is very close to the ideal...
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Updated: Aug 12, 2025

Finite Element Modeling for the Simulation of the Quasi-Static Compression of Corrugated Tapered Tubes
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CHalf: Folding Stability Made Simple.

Chad D Hyer1, Hsien-Jung L Lin1, Connor T Haderlie1

  • 1Department of Chemistry and Biochemistry, Brigham Young University, Provo, Utah84602, United States.

Journal of Proteome Research
|January 27, 2023
PubMed
Summary
This summary is machine-generated.

Researchers can now easily quantify protein folding stability (PFS) using the new C Half software. This tool simplifies PFS analysis, promoting its use in disease research and drug development.

Keywords:
IPSASPROXTPPgraphical user interfaceprotein folding stability

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Area of Science:

  • Proteomics
  • Biochemistry
  • Computational Biology

Background:

  • Protein structure dictates function and integrity, correlating with protein folding stability (PFS).
  • Quantifying PFS offers insights into protein efficacy, quality, and differential stability in disease or ligand-bound states.
  • Current proteomics research predominantly focuses on concentration-based studies, with limited adoption of PFS due to a lack of user-friendly tools.

Purpose of the Study:

  • To introduce C Half, the first user-friendly software with a graphical user interface for calculating protein folding stability (PFS).
  • To lower the barrier to entry for researchers investigating PFS and promote its broader application in scientific studies.

Main Methods:

  • Development of C Half software with a graphical user interface for PFS calculation.
  • Compatibility with both chemical and thermal denaturation folding stability assays.
  • Integration of data visualization tools for analyzing PFS variations across protein sequences and experimental conditions.

Main Results:

  • C Half enables site-specific PFS calculation from chemical denaturation assays.
  • The software supports thermal denaturation folding stability assays.
  • Includes visualization tools for identifying changes in PFS under different conditions.

Conclusions:

  • The C Half software simplifies PFS analysis, making it accessible to a wider research community.
  • Increased utilization of PFS studies is expected to accelerate understanding of disease pathogenesis and pathophysiology.
  • Promoting PFS research can advance the development of diagnostics and therapeutics.