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Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
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Phosphorylation01:02

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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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...
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Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
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Probabilistic Prediction of Protein Phosphorylation Sites Using Classification Relevance Units Machines.

Mark Menor1, Kyungim Baek, Guylaine Poisson

  • 1Department of Information and Computer Sciences, University of Hawai`I at Mānoa 1680 East-West Road, Honolulu, HI 96822, USA.

ACM SIGAPP Applied Computing Review : a Publication of the Special Interest Group on Applied Computing
|October 29, 2013
PubMed
Summary
This summary is machine-generated.

We developed a new computational method, Classification Relevance Units Machine (CRUM), for predicting protein phosphorylation sites. CRUM offers comparable accuracy to SVM but is more efficient for large-scale biological data analysis.

Keywords:
ClassificationKernel machinePhosphorylation

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Area of Science:

  • Biochemistry
  • Computational Biology
  • Bioinformatics

Background:

  • Protein phosphorylation is a crucial post-translational modification regulating cellular processes.
  • Experimental identification of phosphorylation sites is costly and time-consuming.
  • Computational prediction of phosphorylation sites is highly desirable.

Purpose of the Study:

  • To introduce a novel kernel-based probabilistic method, Classification Relevance Units Machine (CRUM), for *in silico* phosphorylation site prediction.
  • To evaluate CRUM's performance and efficiency compared to existing methods like Support Vector Machine (SVM).
  • To explore the impact of different features (BLOSUM encoding, disorder, amino acid composition) on CRUM's predictive accuracy.

Main Methods:

  • Development of a CRUM model for predicting protein phosphorylation sites.
  • Implementation of CRUM using various feature combinations: BLOSUM encoding, protein disorder, and amino acid composition.
  • Evaluation of CRUM predictors using cross-validation and benchmark experiments.

Main Results:

  • CRUM demonstrates predictive performance comparable to SVM but offers a more parsimonious model.
  • CRUM exhibits lower training run-time and memory complexity than Relevance Vector Machine (RVM).
  • CRUM predictors incorporating BLOSUM encoding achieved top performance in cross-validation and benchmark tests.

Conclusions:

  • CRUM is a viable and efficient computational tool for predicting protein phosphorylation sites.
  • The BLOSUM feature significantly enhances CRUM's predictive capabilities.
  • Further improvements in CRUM predictors are possible through comparative studies with existing tools.