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Related Concept Videos

Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

7.0K
Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
7.0K
Preparation and Reactions of Sulfides02:26

Preparation and Reactions of Sulfides

5.3K
Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
5.3K
Structure and Nomenclature of Thiols and Sulfides02:17

Structure and Nomenclature of Thiols and Sulfides

5.3K
Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry,...
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Hydrogen Bonds01:04

Hydrogen Bonds

11.5K
A hydrogen bond is formed when a weakly positive hydrogen atom already bonded to one electronegative atom (for example, the oxygen in the water molecule) is attracted to another electronegative atom from another polar molecule, such as water (H2O), hydrogen fluoride (HF), or ammonia (NH3). The huge electronegativity difference between the H atom (2.1) and the atom to which it is bonded (4.0 for an F atom, 3.5 for an O atom, or 3.0 for an N atom), combined with the very small size of an H atom...
11.5K
Hydrogen Bonds00:26

Hydrogen Bonds

128.3K
Hydrogen bonds are weak attractions between atoms that have formed other chemical bonds. One of these atoms is electronegative, like oxygen, and has a partial negative charge. The other is a hydrogen atom that has bonded with another electronegative atom and has a partial positive charge.
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Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are unequally shared....
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Valence Bond Theory02:45

Valence Bond Theory

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Overview of Valence Bond Theory
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Synthesis of a Thiol Building Block for the Crystallization of a Semiconducting Gyroidal Metal-sulfur Framework
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HaloTag Forms an Intramolecular Disulfide.

Kirsten Deprey1, Joshua A Kritzer1

  • 1Department of Chemistry, Tufts University, Medford, Massachusetts 02155, United States.

Bioconjugate Chemistry
|April 15, 2021
PubMed
Summary
This summary is machine-generated.

HaloTag protein can form internal disulfide bonds under oxidizing conditions. A new mutant, HaloTag8, prevents this disulfide formation while maintaining protein activity for chemical biology applications.

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Area of Science:

  • Biochemistry
  • Chemical Biology
  • Molecular Biology

Background:

  • HaloTag is a versatile protein labeling technology used in various chemical biology applications.
  • Recombinant HaloTag protein is susceptible to forming internal disulfide bonds under oxidizing conditions.

Purpose of the Study:

  • To characterize the internal disulfide bond formation in HaloTag.
  • To identify the cysteine residues involved in this process.
  • To develop a disulfide-bond-resistant HaloTag mutant.

Main Methods:

  • Protein purification and characterization.
  • Disulfide bond analysis under varying redox conditions.
  • Site-directed mutagenesis to create HaloTag variants.

Main Results:

  • HaloTag forms an internal disulfide bond involving specific cysteine residues under oxidizing conditions.
  • A novel mutant, HaloTag8, was engineered to prevent disulfide bond formation.
  • HaloTag8 retains the functional activity of the wild-type HaloTag.

Conclusions:

  • Internal disulfide bond formation can be a concern for recombinant HaloTag, especially in extracellular applications.
  • HaloTag8 offers a solution for researchers needing to avoid this artifact.
  • The findings provide insights into HaloTag protein stability and engineering.