Additional file 1: Figure S1. of Protein aggregation, structural disorder and RNA-binding ability: a new approach for physico-chemical and gene ontology classification of multiple datasets

Autor: Klus, Petr, Ponti, Riccardo, Livi, Carmen, Tartaglia, Gian
Rok vydání: 2015
DOI: 10.6084/m9.figshare.c.3607472_d1.v1
Popis: Physico-chemical determinants of protein insolubility. High-solubility (HS) proteins show A) higher burial in human and mouse, in agreement with the observations reported in the original study. Figure S2. Physico-chemical of C. elegans mutant strains. A) In the hsf-1 strain, highly enriched proteins (HSF 4/4) are less structurally disordered than those poorly enriched (HSF1 1/4). B) In the daf-2 strain (long-lived), highly enriched proteins (DAF2 4/4) show lower beta-sheet propensities than those poorly enriched (DAF2 1/4), in agreement with observations reported in the original experimental study. (DOCX 412 kb)
Databáze: OpenAIRE