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Related Concept Videos

Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Insulin: The Receptor and Signaling Pathways01:28

Insulin: The Receptor and Signaling Pathways

Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but this inhibition is released...
Insulin Secretory Vesicles01:05

Insulin Secretory Vesicles

Insulin secretory vesicles release insulin to stimulate blood glucose uptake and regulate carbohydrate metabolism. When the blood glucose levels increase, glucose enters the pancreatic β-islet cells through glucose transporters. Once inside, glucose is metabolized through glycolysis, the citric acid cycle, and the electron transport chain, producing ATP. This increase in ATP concentration closes ATP-sensitive potassium channels, leading to depolarization of the membrane and the opening of...
Insulin: Biosynthesis, Chemistry, and Preparation01:25

Insulin: Biosynthesis, Chemistry, and Preparation

The endoplasmic reticulum (ER) of pancreatic β-cells synthesizes preproinsulin, which consists of a signal peptide, A and B chains, and a C-peptide. Preproinsulin is then cleaved and folded into proinsulin, which translocates to the Golgi apparatus for sorting and packaging into secretory granules. In these granules, enzymatic clipping generates insulin and C-peptide.
Damage or functional impairment of β-cells inhibits insulin production, leading to diabetes. Diabetes treatment primarily uses...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

Updated: May 21, 2026

Homogeneous Time-resolved Förster Resonance Energy Transfer-based Assay for Detection of Insulin Secretion
07:30

Homogeneous Time-resolved Förster Resonance Energy Transfer-based Assay for Detection of Insulin Secretion

Published on: May 10, 2018

Conformational dynamics of insulin.

Qing-Xin Hua1, Wenhua Jia, Michael A Weiss

  • 1Department of Biochemistry, School of Medicine, Case Western Reserve University Cleveland, OH, USA.

Frontiers in Endocrinology
|June 1, 2012
PubMed
Summary

Insulin

Area of Science:

  • Biochemistry
  • Structural Biology
  • Pharmaceutical Science

Background:

  • Insulin's structure and dynamics are crucial for its function and stability.
  • Understanding monomeric insulin in solution is key to developing improved formulations.

Purpose of the Study:

  • To investigate the solution structure and dynamics of monomeric insulin using insulin lispro as a model.
  • To identify key structural features and dynamic properties relevant to insulin stability and receptor binding.

Main Methods:

  • Nuclear Magnetic Resonance (NMR)-based modeling.
  • Amide-proton exchange kinetics in Deuterium Oxide (D2O).

Main Results:

  • NMR modeling confirmed crystal structure relationships but revealed dynamic anomalies.
Keywords:
NMR spectroscopyamide-proton exchangediabetes mellitushydrogen bondprotein dynamicsprotein engineeringprotein structureprotein therapeutics

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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Homogeneous Time-resolved Förster Resonance Energy Transfer-based Assay for Detection of Insulin Secretion
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  • Most hydrogen bonds in crystal structures are transient in solution.
  • Stable hydrogen bonds are localized to four alpha-helical sites near the internal disulfide bridge.

    • Conclusions:

    • Insulin exhibits significant flexibility on its active surface, potentially aiding receptor binding.
    • Conformational flexibility contributes to pharmaceutical formulation degradation.
    • "Dynamic re-engineering" of insulin could lead to ultra-stable formulations for global health applications.