NDLI: On the segregation of protein ionic residues by charge type

Content Provider	Springer Nature Link
Author	Parker, Michael S. Balasubramaniam, Ambikaipakan Parker, Steven L.
Copyright Year	2012
Abstract	Based on ubiquitous presence of large ionic motifs and clusters in proteins involved in gene transcription and protein synthesis, we analyzed the distribution of ionizable sidechains in a broad selection of proteins with regulatory, metabolic, structural and adhesive functions, in agonist, antagonist, toxin and antimicrobial peptides, and in self-excising inteins and intron-derived proteins and sequence constructs. All tested groups, regardless of taxa or sequence size, show considerable segregation of ionizable sidechains into same type charge (homoionic) tracts. These segments in most cases exceed half of the sequence length and comprise more than two-thirds of all ionizable sidechains. This distribution of ionic residues apparently reflects a fundamental advantage of sorted electrostatic contacts in association of sequence elements within and between polypeptides, as well as in interaction with polynucleotides. While large ionic densities are encountered in highly interactive proteins, the average ionic density in most sets does not change appreciably with size of the homoionic segments, which supports the segregation as a modular feature favoring association.
Starting Page	2231
Ending Page	2247
Page Count	17
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	43
Issue Number	6
e-ISSN	14382199
Language	English
Publisher	Springer Vienna
Publisher Date	2012-10-19
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Ionic segregation Homobasic tract Homoacidic tract Homoionic zipper Neurobiology Life Sciences Proteomics Biochemical Engineering Analytical Chemistry Biochemistry
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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