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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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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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Stereoisomerism of Cyclic Compounds02:33

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In this lesson, we delve into the role of ring conformation and its stability, which determines the spatial arrangement and, consequently, the molecular symmetry and stereoisomerism of cyclic compounds. 1,2-Dimethylcyclohexane is used as a case study to evaluate the possible number of stereoisomers. Here, given the multiple (n = 2) chiral centers, there are 2n = 4 possible configurations that lack a plane of symmetry, as the ring skeleton exists in a non-planar chair conformation. In addition,...
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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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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Stability of Conjugated Dienes01:28

Stability of Conjugated Dienes

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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.
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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Computational insights into the circular permutation roles on ConA binding and structural stability.

Vinicius J S Osterne1, Vanir R Pinto-Junior2,3, Messias V Oliveira2

  • 1Laboratory of Biochemistry and Glycobiology, Department of Biotechnology, Ghent University, 9000, Ghent, Belgium.

Current Research in Structural Biology
|April 1, 2024
PubMed
Summary

The processing of Concanavalin A (ConA) significantly enhances lectin stability, particularly maintaining its tetrameric form. This maturation does not substantially alter ConA

Keywords:
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Concanavalin A (ConA) is a well-studied lectin with diverse applications.
  • The exact purpose of ConA's post-translational processing and circular permutation remains unclear.
  • Understanding these modifications is crucial for elucidating ConA's functional mechanisms.

Purpose of the Study:

  • To investigate the impact of post-translational modifications on ConA stability and carbohydrate-binding properties.
  • To compare the structural and dynamic characteristics of unprocessed ProConA and mature ConA.
  • To elucidate the functional significance of ConA processing.

Main Methods:

  • Utilized 200 ns molecular dynamics simulations for monomeric and oligomeric forms of ProConA and ConA.
  • Analyzed trajectory data for both unbound lectins and complexes with D-mannose and GlcNAc2Man9 N-glycan.
  • Performed comparative analyses of stability parameters, interaction profiles, and binding free energies.

Main Results:

  • ProConA exhibited significantly lower stability parameters compared to ConA at both monomeric and tetrameric levels.
  • Both ProConA and ConA demonstrated similar carbohydrate-binding properties, including interaction profiles and binding free energies.
  • The processing of ProConA enhances the stability of the mature ConA, particularly in maintaining the tetrameric oligomer.

Conclusions:

  • ConA processing plays a critical role in enhancing lectin stability, especially for tetramer formation.
  • Maturation does not significantly alter the fundamental carbohydrate-binding capabilities of ConA.
  • The study provides insights into the functional importance of post-translational modifications in lectin structure and function.