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Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Factors Affecting Protein-Drug Binding: Drug-Related Factors01:18

Factors Affecting Protein-Drug Binding: Drug-Related Factors

Drug binding to proteins is a complex phenomenon influenced by various drug-related factors, each playing a significant role in the interaction between drugs and proteins within the body.
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...
Pore Transport and Ion-Pair Transport01:17

Pore Transport and Ion-Pair Transport

Pore transport and ion-pair formation are critical mechanisms for the absorption and distribution of drugs in the body.
Pore transport, also known as convective transport, is a process where small molecules like urea, water, and sugars rapidly cross cell membranes as though there were channels or pores in the membrane. Although direct microscopic evidence is limited  but the concept of pores or channels is widely accepted based on physiological evidence. Despite the lack of direct microscopic...
Ion-Exchange Chromatography01:09

Ion-Exchange Chromatography

Ion-exchange chromatography, or IEC, is a technique for separating ions based on their affinity for the stationary phase. The stationary phase is a cross-linked polymer resin with covalently attached ionic functional groups. The functional groups can be either positively charged (cation exchangers) or negatively charged (anion exchangers). A cation exchanger consists of a polymeric anion and active cations, while an anion exchanger is a polymeric cation with active anions. The choice of...
Physiological Pharmacokinetic Models: Assumption with Protein Binding01:13

Physiological Pharmacokinetic Models: Assumption with Protein Binding

Physiological models with protein binding in pharmacokinetics offer a sophisticated approach to understanding drug disposition. These models consider drug-protein interactions, enabling them to effectively predict drug concentrations in different organs and tissues. This precision aids in accurate drug dosing, providing a significant advantage over conventional models. A key process within these models is equilibration, which ensures that drug concentrations achieve a steady state within the...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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Related Experiment Video

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Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

Selective and specific ion binding on proteins at physiologically-relevant concentrations.

Linlin Miao1, Haina Qin, Patrice Koehl

  • 1Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore.

FEBS Letters
|September 13, 2011
PubMed
Summary
This summary is machine-generated.

Protein structure is not solely dependent on salt ions. While salt addition did not induce folding in ephrin-B2, specific anions showed high-affinity binding, suggesting a role beyond structural stabilization.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Dynamics

Background:

  • Insoluble proteins often lack well-defined tertiary structures in unsalted water.
  • The role of salt ions in protein folding and stability remains a key question in structural biology.

Purpose of the Study:

  • To investigate if the absence of salt ions causes protein unfolding.
  • To determine the effect of various salts on the structure of the ephrin-B2 cytoplasmic domain.

Main Methods:

  • Solubilization of insoluble ephrin-B2 cytoplasmic domain in unsalted water.
  • Nuclear Magnetic Resonance (NMR) spectroscopy, including HSQC titrations with 14 different salts.

Main Results:

  • Ephrin-B2 was confirmed to be only partially folded in unsalted water.
  • Salt addition did not induce significant protein folding at physiologically relevant ion concentrations.
  • Eight specific anions demonstrated high-affinity and specific binding to ephrin-B2 at biologically relevant concentrations.

Conclusions:

  • Protein structure is not solely dictated by the presence or absence of salt ions.
  • Anion binding to ephrin-B2 is specific and salt-dependent, suggesting roles beyond structural stabilization.
  • Further research is needed to elucidate the functional implications of specific anion-protein interactions.