ReviewProtein science : a publication of the Protein Society2015
ChSeq: A database of chameleon sequences.
Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 59 citations in OpenAlex.
- Chameleon sequences-Structural effects.PloS one · 2025Article
- Chameleon Sequences-Structural Effects in Proteins Characterized by Hydrophobicity Disorder.ACS omega · 2024Article
- Characterization of alternative splicing during mammalian brain development reveals the extent of isoform diversity and potential effects on protein structural changes.Biology open · 2024Article
- In silico design of potential Mcl-1 peptide-based inhibitors.Journal of molecular modeling · 2024Article
- ATLAS: protein flexibility description from atomistic molecular dynamics simulations.Nucleic acids research · 2024Article
- Identification of a covert evolutionary pathway between two protein folds.Nature communications · 2023Article
- Design and characterization of a protein fold switching network.Nature communications · 2023Article
- Many dissimilar NusG protein domains switch between α-helix and β-sheet folds.Nature communications · 2022Article
- Information quantity for secondary structure propensities of protein subsequences in the Protein Data Bank.Biophysics and physicobiology · 2022Article
- AlphaFold 2: Why It Works and Its Implications for Understanding the Relationships of Protein Sequence, Structure, and Function.Journal of chemical information and modeling · 2021Article
- A sequence-based method for predicting extant fold switchers that undergo α-helix ↔ β-strand transitions.Biopolymers · 2021Article
- The role of local versus nonlocal physicochemical restraints in determining protein native structure.Current opinion in structural biology · 2021Review
- The 'Shape-Shifter' Peptide from the Disulphide Isomerase PmScsC Shows Context-Dependent Conformational Preferences.Biomolecules · 2021Article
- α-CGRP disrupts amylin fibrillization and regulates insulin secretion: implications on diabetes and migraine.Chemical science · 2021Article
- Structure of the Hydrophobic Core Determines the 3D Protein Structure-Verification by Single Mutation Proteins.Biomolecules · 2020Article
- Protein Secondary Structure Prediction Based on Data Partition and Semi-Random Subspace Method.Scientific reports · 2018Article
- Unfolding the Mysteries of Protein Metamorphosis.ACS chemical biology · 2018Review
- Sixty-five years of the long march in protein secondary structure prediction: the final stretch?Briefings in bioinformatics · 2018Article
- The presence of non-native helical structure in the unfolding of a beta-sheet protein MPT63.Protein science : a publication of the Protein Society · 2017Article
- The role of negative selection in protein evolution revealed through the energetics of the native state ensemble.Proteins · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Chameleon sequences (ChSeqs) refer to sequence strings of identical amino acids that can adopt different conformations in protein structures. Researchers have detected and studied ChSeqs to understand the interplay between local and global interactions in protein structure formation. The different secondary structures adopted by one ChSeq challenge sequence-based secondary structure predictors. With increasing numbers of available Protein Data Bank structures, we here identify a large set of ChSeqs ranging from 6 to 10 residues in length. The homologous ChSeqs discovered highlight the structural plasticity involved in biological function. When compared with previous studies, the set of unrelated ChSeqs found represents an about 20-fold increase in the number of detected sequences, as well as an increase in the longest ChSeq length from 8 to 10 residues. We applied secondary structure predictors on our ChSeqs and found that methods based on a sequence profile outperformed methods based on a single sequence. For the unrelated ChSeqs, the evolutionary information provided by the sequence profile typically allows successful prediction of the prevailing secondary structure adopted in each protein family. Our dataset will facilitate future studies of ChSeqs, as well as interpretations of the interplay between local and nonlocal interactions. A user-friendly web interface for this ChSeq database is available at prodata.swmed.edu/chseq.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.