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Chromatin immunoprecipitation, or ChIP, is an antibody-based technique used to identify sites on DNA that bind to transcription factors of interest or histone proteins. It also helps determine the type of histone modifications such as acetylation, phosphorylation, or methylation.
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Genome-wide Snapshot of Chromatin Regulators and States in Xenopus Embryos by ChIP-Seq
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ChSeq: A database of chameleon sequences.

Wenlin Li1,2, Lisa N Kinch3, P Andrew Karplus4

  • 1Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, Texas, 75390-9050.

Protein Science : a Publication of the Protein Society
|May 14, 2015
PubMed
Summary
This summary is machine-generated.

Chameleon sequences (ChSeqs), amino acid strings with flexible structures, were extensively identified. These sequences challenge secondary structure prediction, but profile-based methods show promise.

Keywords:
ChSeqbiological functionchameleon sequenceconformational changesecondary structuresecondary structure predictionsequence profilestructural plasticity

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Chameleon sequences (ChSeqs) are identical amino acid segments adopting diverse protein conformations.
  • Understanding ChSeqs is crucial for deciphering protein structure formation and the interplay of local and global interactions.
  • Existing secondary structure prediction methods struggle with the conformational variability of ChSeqs.

Purpose of the Study:

  • To identify and characterize a comprehensive dataset of ChSeqs.
  • To evaluate the performance of sequence-based secondary structure prediction methods on ChSeqs.
  • To provide a resource for future research on ChSeqs and protein structural plasticity.

Main Methods:

  • Utilized the Protein Data Bank to identify ChSeqs of 6-10 amino acid residues.
  • Compared homologous and unrelated ChSeqs to assess structural plasticity.
  • Applied sequence profile-based and single-sequence-based secondary structure predictors to the identified ChSeqs.

Main Results:

  • Discovered a large dataset of ChSeqs, significantly expanding previous findings.
  • Identified unrelated ChSeqs with lengths up to 10 residues, a notable increase.
  • Sequence profile-based predictors outperformed single-sequence methods, accurately predicting prevailing secondary structures for unrelated ChSeqs.

Conclusions:

  • The identified ChSeq dataset offers a valuable resource for studying protein structural plasticity.
  • Evolutionary information in sequence profiles aids in predicting secondary structures for conformationally flexible regions.
  • This work enhances our understanding of the relationship between sequence, structure, and function.