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• W2114823344 endingPage "427" @default.
• W2114823344 startingPage "415" @default.
• W2114823344 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. Proteins 2000;41:415–427. © 2000 Wiley-Liss, Inc." @default.
• W2114823344 created "2016-06-24" @default.
• W2114823344 creator A5041279840 @default.
• W2114823344 creator A5061603180 @default.
• W2114823344 creator A5083199032 @default.
• W2114823344 date "2000-01-01" @default.
• W2114823344 modified "2023-10-11" @default.
• W2114823344 title "Why are ?natively unfolded? proteins unstructured under physiologic conditions?" @default.
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• W2114823344 doi "https://doi.org/10.1002/1097-0134(20001115)41:3<415::aid-prot130>3.0.co;2-7" @default.
• W2114823344 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11025552" @default.
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