Binding Thermodynamics to Intrinsically Disordered Protein Domains.

Arne Schön, Ernesto Freire

Abstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

2 authors.

Arne SchönDepartment of Biology, The Johns Hopkins University, Baltimore, MD, USA.

Ernesto FreireDepartment of Biology, The Johns Hopkins University, Baltimore, MD, USA. ef@jhu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many proteins are intrinsically disordered or contain one or more disordered domains. These domains can participate in binding interactions with other proteins or small ligands. Binding to intrinsically disordered protein domains requires the folding or structuring of those regions such that they can establish well-defined stoichiometric interactions. Since, in such a situation binding is coupled to folding, the energetics of those two events is reflected in the measured binding thermodynamics. In this protocol, we illustrate the thermodynamic differences between binding coupled to folding and binding independent of folding for the same protein. As an example, we use the HIV-1 envelope glycoprotein gp120 that contains structured as well as disordered domains. In the experiments presented, the binding of gp120 to molecules that bind to disordered regions and trigger structuring (CD4 or MAb 17b) and to molecules that bind to structured regions and do not induce conformational structuring (MAb b12) is discussed.

Indexed as

Antibodies, MonoclonalAntigen-Antibody ReactionsCalorimetryCD4 AntigensHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansIntrinsically Disordered ProteinsProtein BindingProtein DomainsProtein FoldingTemperatureThermodynamicsAntibodies, MonoclonalCD4 Antigensgp120 protein, Human immunodeficiency virus 1HIV AntibodiesHIV Envelope Protein gp120Intrinsically Disordered ProteinsCalorimetryFolding upon bindinggp120HIVIDPInteractionsITCProtein folding

Identifiers

PMID32696371

DOI10.1007/978-1-0716-0524-0_22

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.