The melting of human plasma fibronectin and its proteolytic fragments has been studied by scanning microcalorimetry to reveal co-operative structural domains in the molecule. It has been established that each of the two similar polypeptide chains of fibronectin has at least 12 structural domains, which differ in stability, size and function. Many of the domains in the N-terminal half of the polypeptide chains appear to be composed of two homologous repeat modules that co-operate to form a single co-operative unit. In the intact fibronectin molecule, the C-terminal regions of both chains seem to interact forming a stable co-operative block. Study holds ProTherm entries: 7447, 7448, 7449, 7450, 7451, 7452, 7453, 7454, 7455, 7456, 7457, 7458 Extra Details:
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:34 p.m.
|Number of data points||24|
|Proteins||Fibronectin ; Fibronectin|
|Assays/Quantities/Protocols||Experimental Assay: dHcal pH:8.0 ; Experimental Assay: Tm pH:8.0 ; Experimental Assay: dHcal pH:7.4 ; Experimental Assay: Tm pH:7.4 ; Experimental Assay: dHcal pH:4.0 ; Experimental Assay: Tm pH:4.0|
|Libraries||Mutations for sequence VSDVPRDLEVVAATPTSLLISWDAPAVTVRYYRITYGETGGNSPVQEFTVPGSKSTATISGLKPGVDYTITVYAVTGRGDSPASSKPISINYRT|