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Conformity

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Conformity is the change in a person’s behavior to go along with the group, even if that person does not agree with the group.

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Unlike ethane and propane that have only two major conformations, butane has more than two conformers. The staggered form of butane in which the bulky methyl groups on the two carbons are placed on opposite sides, that is, at a dihedral angle of 180°, is the lowest energy, most stable form — called the anti conformer. This conformation is stabilized due to the absence of steric repulsion between the largely spaced out methyl groups. The other two staggered conformations are...

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Adolf von Baeyer attempted to explain the instabilities of small and large cycloalkane rings using the concept of angle strain — the strain caused by the deviation of bond angles from the ideal 109.5° tetrahedral value for sp3 hybridized carbons. However, while cyclopropane and cyclobutane are strained, as expected from their highly compressed bond angles, cyclopentane is more strained than predicted, and cyclohexane is virtually strain-free. Hence, Baeyer’s theory that...

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In an organic molecule, free rotation about the carbon-carbon single bond results in energetically different conformers of the molecule. Due to this rotation, called the internal rotation, ethane has two major conformations — staggered and eclipsed.
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Related Experiment Video

Updated: Feb 14, 2026

Spatial Separation of Molecular Conformers and Clusters

Spatial Separation of Molecular Conformers and Clusters

Published on: January 9, 2014

Confirmation for conformational selection.

Yajun Jiang¹, Charalampos G Kalodimos¹

¹Department of Structural Biology, St Jude Children's Research Hospital, Memphis, United States.

|February 21, 2018

Summary

Nuclear Magnetic Resonance (NMR) studies have resolved a key question regarding how Hsp70 chaperones recognize their protein substrates. These findings clarify the molecular mechanisms involved in substrate binding and recognition by this essential protein family.

Keywords:

E. coli Hsp70 biophysics conformational selection induced fit methyl-TROSY NMR molecular chaperones structural biology

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Spatial Separation of Molecular Conformers and Clusters

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Published on: January 9, 2014

G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Hsp70 chaperones are essential proteins involved in various cellular processes, including protein folding and degradation.
Understanding how Hsp70 chaperones recognize diverse substrates is crucial for deciphering their biological functions.
A long-standing debate exists regarding the precise mechanism of substrate recognition by Hsp70.

Purpose of the Study:

To elucidate the molecular mechanism by which Hsp70 chaperones recognize and bind to their substrates.
To provide definitive evidence settling a part of the ongoing debate on Hsp70 substrate recognition.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy was employed to study the interaction between Hsp70 and its substrates.
Detailed structural and dynamic analyses were performed using NMR data.

Main Results:

NMR studies provided critical insights into the Hsp70 substrate binding interface.
The results clarify specific aspects of the Hsp70-substrate recognition mechanism, resolving part of a long-standing debate.

Conclusions:

The findings contribute to a deeper understanding of Hsp70 chaperone function at a molecular level.
This work settles a specific aspect of the Hsp70 substrate recognition mechanism, paving the way for future research.