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Related Concept Videos

Stability of Conjugated Dienes01:28

Stability of Conjugated Dienes

Introduction
A comparison of the enthalpies of hydrogenation of dienes reveals that conjugated dienes release less heat on hydrogenation, rendering them more stable than their nonconjugated analogs.
Complexation Equilibria: Factors Influencing Stability of Complexes01:09

Complexation Equilibria: Factors Influencing Stability of Complexes

In complexation reactions, metal cations are the electron pair acceptors, and the ligands are the electron pair donors. The stability of the metal complexes depends primarily on the complexing ability of the central metal ion and the nature of the ligands. Generally, the complexing ability of the metal ion depends on the size and charge of the ion. As the metal ion size increases, the stability of the metal complexes decreases, provided that the valency of the metal ion and the ligands remain...
Stability of Equilibrium Configuration01:23

Stability of Equilibrium Configuration

Understanding the stability of equilibrium configurations is a fundamental part of mechanical engineering. In any system, there are three distinct types of equilibrium: stable, neutral, and unstable.
A stable equilibrium occurs when a system tends to return to its original position when given a small displacement, and the potential energy is at its minimum. An example of a stable equilibrium is when a cantilever beam is fixed at one end and a weight is attached to the other end. If the weight...
Stability of Substituted Cyclohexanes02:30

Stability of Substituted Cyclohexanes

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...
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
Stability of structures01:14

Stability of structures

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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Updated: Jun 12, 2026

Isolating Free Carbenes, their Mixed Dimers and Organic Radicals
10:44

Isolating Free Carbenes, their Mixed Dimers and Organic Radicals

Published on: April 19, 2019

Stability and CDR composition biases enrich binder functionality landscapes.

Benjamin J Hackel1, Margaret E Ackerman, Shanshan W Howland

  • 1Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

Journal of Molecular Biology
|June 15, 2010
PubMed
Summary
This summary is machine-generated.

Developing protein libraries requires balancing diversity and stability. A new strategy combining structural bias and tailored amino acid composition significantly improved the selection of functional molecular binders.

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The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)
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The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)

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Last Updated: Jun 12, 2026

Isolating Free Carbenes, their Mixed Dimers and Organic Radicals
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Published on: April 19, 2019

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)
07:22

The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)

Published on: January 12, 2024

Area of Science:

  • Protein engineering and molecular recognition

Background:

  • Evolving protein function is challenging due to the complex sequence-function landscape.
  • Protein library diversification must balance exploring new functions with maintaining protein stability and expression.

Purpose of the Study:

  • To explore sequence-function relationships in protein libraries for molecular recognition.
  • To investigate the impact of two sequence diversification strategies on an immunoglobulin (Ig) scaffold library based on the fibronectin type III domain.

Main Methods:

  • Identified structurally important paratope positions through stability, structural, and phylogenetic analyses.
  • Implemented two diversification strategies: partial wild-type conservation and tailored amino acid composition mimicking antibody binding sites.
  • Compared three library designs (random, DE loop biased, and 11-position structurally biased with antibody-inspired diversity) using pooled library competition.

Main Results:

  • The library with structural bias and tailored diversity yielded 19 out of 21 successful binders against seven targets.
  • Sequence analysis confirmed the importance of both tailored compositional diversity and structural bias for successful molecular recognition.
  • Selection of clones with varying expression levels further elucidated the role of structural bias.

Conclusions:

  • A strategy combining structural bias at critical positions and tailored amino acid composition enhances the evolution of protein binders.
  • This approach effectively navigates the protein sequence-function landscape for improved molecular recognition capabilities.