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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Factors Affecting Protein-Drug Binding: Protein-Related Factors01:20

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Drug binding to proteins is a key aspect of pharmacokinetics and can influence a drug's distribution, absorption, and elimination in the body. Several factors, including the drug's physiochemical properties, protein concentration, disease states, and the number of binding sites on the protein, influence this process.
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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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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Drug Distribution: Plasma Protein Binding01:29

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Drugs predominantly attach to plasma proteins, with only a small percentage remaining unbound. The unbound portion can be calculated as one minus the bound fraction. Acidic drugs form large, inactive complexes by reversibly binding to plasma albumin, which prevents them from diffusing across biological barriers. These drug-protein complexes act as reservoirs for the drugs. As the concentration of unbound drugs decreases, these complexes quickly dissociate to release the free drug, maintaining...
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Protein-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

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Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
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Related Experiment Video

Updated: Feb 3, 2026

Analysis of AtHIRD11 Intrinsic Disorder and Binding Towards Metal Ions by Capillary Gel Electrophoresis and Affinity Capillary Electrophoresis
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PreSMo Target-Binding Signatures in Intrinsically Disordered Proteins.

Do-Hyoung Kim1, Kyou-Hoon Han1

  • 1Genome Editing Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, 34141, Korea.

Molecules and Cells
|October 24, 2018
PubMed
Summary

Intrinsically disordered proteins (IDPs) lack stable structures but perform vital functions and cause diseases. Pre-structured motifs (PreSMos) explain how IDPs bind targets, offering a structural basis for their function.

Keywords:
IDPsIDR (Intrinsically Disordered Region)IUPs (Intrinsically Unfolded Proteins)NMRPreSMos (Pre-Structured Motifs)

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Intrinsically disordered proteins (IDPs) challenge the classical structure-function paradigm.
  • IDPs lack stable 3D structures yet are crucial for biological functions and implicated in diseases like cancer and neurodegeneration.

Purpose of the Study:

  • To review the developmental history and characteristics of Pre-structured motifs (PreSMos).
  • To elucidate the role of PreSMos in intrinsically disordered protein target binding.
  • To present newly discovered PreSMos and their functional relevance.

Main Methods:

  • Literature review on PreSMo discovery and characterization.
  • Analysis of structural and functional data for IDPs and PreSMos.

Main Results:

  • PreSMos are transient local secondary structures in IDPs.
  • PreSMos are critical determinants for IDP target binding.
  • The PreSMo concept offers an atomic-resolution explanation for IDP-target interactions.

Conclusions:

  • PreSMos provide a key structural insight into the function of intrinsically disordered proteins.
  • Understanding PreSMos is crucial for comprehending IDP roles in health and disease.
  • This work highlights the significance of PreSMos in protein science.