The respective roles of polar/nonpolar binary patterns and amino acid composition in protein regular secondary structures explored exhaustively using hydrophobic cluster analysis-Reference-Cited by-同舟云学术

The respective roles of polar/nonpolar binary patterns and amino acid composition in protein regular secondary structures explored exhaustively using hydrophobic cluster analysis

Published:2016-03-09 Issue:5 Volume:84 Page:624-638
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Rebehmed Joseph¹,Quintus Flavien¹,Mornon Jean-Paul¹,Callebaut Isabelle¹

Affiliation:

1. CNRS UMR7590; Sorbonne Universités, Université Pierre Et Marie Curie-Paris6 - MNHN - IRD - IUC; Paris France

Funder

Institut National Du Cancer

Agence Nationale de la Recherche - France

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference36 articles.

1. Correlation between observed transcripts and sequenced orfs of chromosome-iii of Saccharomyces-cerevisiae;Tanaka;Nucleic Acids Res,1993

2. Finding families for genomic ORFans;Fischer;Bioinformatics,1999

3. Orphans and new gene origination, a structural and evolutionary perspective;Light;Curr Opin Struct Biol,2014

4. A comprehensive repertoire of foldable segments within genomes;Faure;PLoS Comput Biol,2013

5. Twilight zone of protein sequence alignments;Rost;Protein Eng,1999

Cited by 11 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Graphene-based Nanocomposites for Amino Acid Sensing;Graphene-based Nanocomposite Sensors;2023-10-13

2. A sequence‐based foldability score combined with AlphaFold2 predictions to disentangle the protein order/disorder continuum;Proteins: Structure, Function, and Bioinformatics;2022-11-09

3. Casein micelle structure and stability;Milk Proteins;2020

4. A topology-based investigation of protein interaction sites using Hydrophobic Cluster Analysis;Biochimie;2019-12

5. Sequence characteristics responsible for protein‐protein interactions in the intrinsically disordered regions of caseins, amelogenins, and small heat‐shock proteins;Biopolymers;2019-07-08