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Related Concept Videos

Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

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Related Experiment Video

Updated: May 10, 2026

Protein Engineering by Yeast Surface Display
05:49

Protein Engineering by Yeast Surface Display

Published on: November 29, 2024

Scientific Laudatio for Professor Andreas Engel.

Dimitrios Fotiadis1, Shirley A Müller2, Daniel J Müller3

  • 1Institute of Biochemistry and Molecular Medicine, University of Bern, 3012 Bern, Switzerland.

Journal of Structural Biology
|May 8, 2026
PubMed
Summary
This summary is machine-generated.

Pioneering scientist Andreas Engel revolutionized structural biology and biophysics. His work in electron microscopy and atomic force microscopy advanced understanding of biological macromolecules and protein complexes.

Keywords:
Andreas EngelAtomic force microscopyElectron crystallographyScanning transmission electron microscopyScientific Laudatio

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Last Updated: May 10, 2026

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Area of Science:

  • Structural Biology
  • Biophysics
  • Macromolecular Visualization

Background:

  • The passing of Andreas Engel marks a significant loss to the scientific community.
  • Engel had a distinguished career spanning over five decades.

Purpose of the Study:

  • To acknowledge the profound impact of Andreas Engel's scientific contributions.
  • To highlight his role in advancing nanoscale visualization of biological structures.

Main Methods:

  • Pioneering contributions to scanning transmission electron microscopy (STEM).
  • Advancements in atomic force microscopy (AFM).
  • Innovations in electron crystallography.

Main Results:

  • Fundamentally shaped the visualization and understanding of biological macromolecules.
  • Opened new avenues for studying membrane protein architecture and function.
  • Advanced the study of supramolecular complexes.

Conclusions:

  • Andreas Engel's legacy lies in his transformative influence on structural biology and biophysics.
  • His work continues to inspire and guide research in macromolecular structure and function.