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Related Concept Videos

Chair Conformation of Cyclohexane02:02

Chair Conformation of Cyclohexane

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 staggered...
Formal Charges02:42

Formal Charges

In some cases, there are seemingly more than one valid Lewis structures for molecules and polyatomic ions. The concept of formal charges can be used to help predict the most appropriate Lewis structure when more than one reasonable structure exists.
Introduction to force01:25

Introduction to force

Consider water flowing from a nozzle to a turbine vane. As the water hits the turbine vane, it exerts a force that causes it to move along the flow of direction. Force is an impact that changes an object's motion, shape, or orientation. Forces can be caused by physical contact, such as a push or pull, or through non-contact interactions, such as magnetic or gravitational forces. Force is a vector quantity with both magnitude and direction, and is measured in newtons (N) in the SI unit system.
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Directing and Steric Effects in Disubstituted Benzene Derivatives01:18

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When disubstituted benzenes undergo electrophilic substitution, the product distribution depends on the directing effect of both substituents. When the directing effects of both substituents reinforce each other, a single product is obtained. For example, bromination of p-nitrotoluene occurs ortho to the methyl group and meta to the nitro group, which is the same position, resulting in a single product. However, if the directing effects of the two groups oppose each other, the more strongly...

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Chairman's introductory remarks

W E Parish1

  • 1Unilever Research & Engineering, Environmental Safety Laboratory, Colworth House, Sharnbrook, Bedford MK44 1LQ, UK.

Toxicology in Vitro : an International Journal Published in Association with BIBRA
|August 13, 2010
PubMed
Summary

No abstract available in PubMed .

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