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Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Immunoprecipitation01:20

Immunoprecipitation

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Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
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Protein-protein Interfaces02:04

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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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Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
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PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins
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PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

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Protocol to process crosslinking and immunoprecipitation data into annotated binding sites.

Shuhao Xu1, Grady G Nguyen1, Jack T Naritomi1

  • 1Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92037, USA; Sanford Stem Cell Institute and Stem Cell Program, University of California, San Diego, La Jolla, CA 92037, USA; Institute for Genomic Medicine, UCSD Stem Cell Program, University of California, San Diego, La Jolla, CA 92037, USA.

STAR Protocols
|April 26, 2024
PubMed
Summary
This summary is machine-generated.

This study introduces Skipper, a computational pipeline for analyzing crosslinking and immunoprecipitation (CLIP) data to identify RNA-binding sites. The protocol enables reproducible mapping of binding sites and downstream analysis from raw CLIP sequencing data.

Keywords:
BioinformaticsGene ExpressionGenomicsRNA-seqSequence analysis

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Area of Science:

  • Molecular Biology
  • Bioinformatics
  • Genomics

Background:

  • Crosslinking and immunoprecipitation (CLIP) is a powerful technique for identifying RNA-binding sites of proteins.
  • Analyzing CLIP data to pinpoint precise binding locations and assess enrichment can be computationally challenging.

Purpose of the Study:

  • To present a detailed protocol for processing and analyzing CLIP data using the Skipper computational pipeline.
  • To enable researchers to map reproducible RNA-binding sites and perform downstream analyses.

Main Methods:

  • The Skipper pipeline partitions annotated transcript regions for analysis.
  • A beta-binomial model is fitted to the data to identify windows of enriched binding.
  • The protocol guides users from raw CLIP data to reproducible binding site identification.

Main Results:

  • The protocol facilitates the mapping of reproducible RNA-binding sites from CLIP data.
  • Enriched binding windows can be reliably called and used for further investigation.
  • The pipeline supports customizable options for diverse research applications.

Conclusions:

  • Skipper provides a robust and adaptable protocol for CLIP data analysis.
  • This method enhances the ability to identify and analyze RNA-protein interactions.
  • The protocol aims to streamline the process of discovering RNA-binding sites.