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Related Concept Videos

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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
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,...

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High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

Sequence correlations shape protein promiscuity.

David B Lukatsky1, Ariel Afek, Eugene I Shakhnovich

  • 1Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel. lukatsky@bgu.ac.il

The Journal of Chemical Physics
|August 17, 2011
PubMed
Summary
This summary is machine-generated.

Diagonal correlations in protein sequences boost promiscuity, or nonspecific binding. This finding explains observed patterns in eukaryotic proteomes and suggests experimental validation.

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Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Science

Background:

  • Protein sequences contain patterns of amino acid clustering.
  • These patterns, termed diagonal correlations, are observed in biological systems.
  • The functional implications of these correlations are not fully understood.

Purpose of the Study:

  • To analytically predict the effect of diagonal correlations on protein binding.
  • To investigate the relationship between sequence patterns and protein promiscuity.
  • To provide a theoretical explanation for observed correlations in proteomes.

Main Methods:

  • Analytical prediction of protein binding propensity.
  • Statistical analysis of sequence patterns (diagonal correlations).
  • Assessment of robustness across different interaction potentials and compositions.

Main Results:

  • Diagonal correlations statistically enhance protein propensity for nonspecific binding (promiscuity).
  • The effect is robust to variations in interaction potentials and amino acid composition.
  • Provides a theoretical basis for enhanced diagonal correlations in eukaryotic proteome hubs.

Conclusions:

  • Diagonal correlations are a key factor influencing protein promiscuity.
  • The findings offer insights into protein function and evolution.
  • Experimental verification of the predicted effect is proposed.