The role of conserved proline residues in fibronectin type III (fnIII) domains is investigated. Surprisingly, none of the standard set of explanations for residue conservation applies. The proline residues are not apparently conserved for function, or stability, or to nucleate folding, or to promote stabilising interactions across domain boundaries. However, when the most highly conserved proline residues are mutated to alanine there is an increase in the rate of aggregation of a fnIII double-module construct. The results suggest that proline residues may be conserved at domain-domain boundaries in fnIII domains to prevent aggregation in multi-modular proteins. Study holds ProTherm entries: 15248, 15249 Extra Details: fibronectin type III; proline; protein stability; protein folding; domain-domain interactions
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:46 p.m.
|Number of data points||2|
|Proteins||Fibronectin ; Fibronectin|
|Assays/Quantities/Protocols||Experimental Assay: ddG_H2O|
|Libraries||Mutations for sequence VSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRT|