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Why are "natively unfolded" proteins unstructured under physiologic conditions?

Authors
  • Uversky, V N
  • Gillespie, J R
  • Fink, A L
Type
Published Article
Journal
Proteins: Structure, Function, and Bioinformatics
Publisher
Wiley
Publication Date
Nov 15, 2000
Volume
41
Issue
3
Pages
415–427
Identifiers
PMID: 11025552
Source
Medline
License
Unknown

Abstract

"Natively unfolded" proteins occupy a unique niche within the protein kingdom in that they lack ordered structure under conditions of neutral pH in vitro. Analysis of amino acid sequences, based on the normalized net charge and mean hydrophobicity, has been applied to two sets of proteins: small globular folded proteins and "natively unfolded" ones. The results show that "natively unfolded" proteins are specifically localized within a unique region of charge-hydrophobicity phase space and indicate that a combination of low overall hydrophobicity and large net charge represent a unique structural feature of "natively unfolded" proteins.

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