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Related Concept Videos

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
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...
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,...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

Updated: Jun 24, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Frameworks for understanding long-range intra-protein communication.

Matthew J Whitley1, Andrew L Lee

  • 1Department of Biochemistry & Biophysics, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA.

Current Protein & Peptide Science
|April 10, 2009
PubMed
Summary
This summary is machine-generated.

Intra-protein communication, crucial for biological processes, is explored through mechanical linkage and dynamic microstate frameworks. Nuclear magnetic resonance (NMR) spectroscopy and network analysis offer insights into protein structure and function.

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Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Related Experiment Videos

Last Updated: Jun 24, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
07:19

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Intra-protein communication is vital for biological processes like allostery and signaling.
  • Despite recent progress, the physical origins of intra-protein communication remain incompletely understood.
  • Existing frameworks offer distinct perspectives on how information propagates within proteins.

Purpose of the Study:

  • To review contemporary frameworks for understanding intra-protein communication.
  • To discuss the successes and shortcomings of these frameworks.
  • To highlight the role of Nuclear Magnetic Resonance (NMR) spectroscopy and network analysis in studying intra-protein communication.

Main Methods:

  • Review of mechanical linkage and dynamic microstate frameworks for intra-protein communication.
  • Application of Nuclear Magnetic Resonance (NMR) spectroscopy to study protein dynamics and thermodynamics.
  • Graph and network theoretic analyses to map protein architecture and connectivity.

Main Results:

  • Proteins exhibit 'small world' network characteristics with both local and long-range residue connectivities.
  • NMR spectroscopy provides insights into both mechanical and thermodynamic aspects of intra-protein communication.
  • Lack of experimental validation for the role of long-range interaction pathways in macroscopic protein characteristics.

Conclusions:

  • Contemporary frameworks offer complementary views on intra-protein communication.
  • Integrated approaches combining mechanical, thermodynamic, and network analyses can enhance understanding.
  • Further experimental studies are needed to validate computational findings on long-range interactions.