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Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Aldehydes and Ketones with Alcohols: Hemiacetal Formation

Aldehydes and Ketones with Alcohols: Hemiacetal Formation

Similar to water, alcohols can add to the carbonyl carbon of the aldehydes and ketones. The addition of one molecule of alcohol to the carbonyl compound forms the hemiacetal or half acetal. As depicted below, in a hemiacetal, the carbon is directly linked to an OH and OR group.

Preparation of Alcohols via Addition Reactions

Preparation of Alcohols via Addition Reactions

Overview
The acid-catalyzed addition of water to the double bond of alkenes is a large-scale industrial method used to synthesize low-molecular-weight alcohols. An acidic atmosphere is required to allow the hydrogen in the water molecule to act as an electrophile and attack the double bond in an alkene. The addition of a proton to the double bond creates a carbocation intermediate. The proton preferentially bonds to the less substituted end of the double bond to create a more stable carbocation...

Conversion of Alcohols to Alkyl Halides

Conversion of Alcohols to Alkyl Halides

This lesson delves into the conversion of alcohols to corresponding alkyl halides and the mechanism of action for different reagents. Typically, the hydroxyl group is first protonated to convert it to a stable leaving group. Consequently, based on the starting alcohol, the mechanism undergoes either of the nucleophilic substitution routes, SN1 or SN2. Tertiary alkyl halides are made using the two-step SN1 mechanism that occurs via a carbocation intermediate, which is stabilized by...

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Related Experiment Video

Updated: Jul 16, 2026

Interactive Molecular Model Assembly with 3D Printing

Interactive Molecular Model Assembly with 3D Printing

Published on: August 13, 2020

Alternative membrane protein conformations in alcohols.

D E Otzen¹, P Sehgal, L W Nesgaard

¹Department of Life Sciences, Aalborg University, Sohngaardsholmsvej 49, DK-9000 Aalborg, Denmark. dao@bio. aau.dk

|March 21, 2007

Summary

Alcohols directly impact membrane protein stability and solubility. They can cause protein precipitation and lead to non-native structures, hindering reversible studies.

Area of Science:

Biochemistry
Membrane protein biophysics
Protein aggregation

Background:

Alcohols are known to affect lipid bilayers and membrane protein oligomerization.
The direct effects of alcohol-water mixtures on membrane protein stability and solubility require further investigation.

Purpose of the Study:

To investigate the direct impact of alcohol-water mixtures on the stability and solubility of membrane proteins.
To understand the conformational changes and aggregation states induced by alcohols.

Main Methods:

Studied detergent-solubilized alpha-helical membrane proteins (DsbB and NhaA) in varying alcohol-water mixtures.
Utilized thioflavin T dye binding and atomic force microscopy (AFM) to characterize protein states.
Assessed protein helicity and solubility at different alcohol concentrations.

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Main Results:

Intermediate alcohol concentrations induced protein precipitation with increased beta-sheet structure, suggesting early fibrillation.
Higher alcohol concentrations led to resolubilization into non-native conformations with altered helicity.
The induced conformational changes were largely irreversible upon alcohol dilution.
Protein precipitation and destabilization correlated with alcohol hydrophobicity.

Conclusions:

Alcohols directly perturb membrane proteins by solvating hydrophobic regions, leading to aggregation at intermediate concentrations.
Resolubilization depends on the dielectric constant and specific alcohol properties.
Alcohols can access diverse membrane protein conformations but are unsuitable for reversible denaturation studies.