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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

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Related Experiment Video

Updated: Jun 5, 2026

Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy

Published on: August 6, 2018

Dissection of complex molecular recognition interfaces.

Christopher A Hunter1, Maria Cristina Misuraca, Simon M Turega

  • 1Department of Chemistry, University of Sheffield, Sheffield S3 7HF, United Kingdom. c.hunter@sheffield.ac.uk

Journal of the American Chemical Society
|December 23, 2010
PubMed
Summary
This summary is machine-generated.

This study quantifies intramolecular hydrogen bonds in supramolecular complexes. Results show these bonds are additive and their effectiveness depends on the chemical structure, not just geometry.

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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
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Hand Controlled Manipulation of Single Molecules via a Scanning Probe Microscope with a 3D Virtual Reality Interface

Published on: October 2, 2016

Area of Science:

  • Supramolecular Chemistry
  • Chemical Biology
  • Physical Chemistry

Background:

  • Supramolecular complexes are formed by non-covalent interactions.
  • Hydrogen bonds play a crucial role in molecular recognition and self-assembly.
  • Understanding the quantitative contributions of individual interactions is key to designing complex molecular systems.

Purpose of the Study:

  • To synthesize and characterize a series of zinc porphyrin-pyridine supramolecular complexes with varying numbers of intramolecular hydrogen bonds.
  • To quantitatively assess the contributions of individual hydrogen bonds to the overall stability and assembly of these complexes.
  • To investigate the relationship between molecular structure, hydrogen bonding, and cooperativity in complex molecular recognition interfaces.

Main Methods:

  • Synthesis of zinc porphyrin and pyridine ligands with peripheral hydrogen-bonding groups.
  • Automated UV/vis titration to characterize 120 different supramolecular complexes.
  • Construction of chemical double mutant cycles to quantify intramolecular hydrogen-bonding interactions and effective molarity (EM).

Main Results:

  • Free energy contributions of individual hydrogen bonds are additive and show little variation with supramolecular architecture.
  • Intramolecular hydrogen bonds are absent when geometrically impossible; excellent complementarity does not guarantee high affinity.
  • Effective molarity for intramolecular carboxylate ester-phenol H-bonds (200 mM) is an order of magnitude higher than for phosphonate diester-phenol H-bonds (30 mM).

Conclusions:

  • The study reveals that intramolecular hydrogen bonds are additive and their impact on assembly is largely independent of architecture.
  • Geometric complementarity alone does not dictate high binding affinity, and conformational flexibility has limited influence on effective molarity.
  • Significant differences in effective molarity between H-bond types suggest a compensation effect, where stronger bonds impose stricter geometric constraints, impacting formation efficiency.