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Interacting processes in protein coagulation
Author(s) -
San Biagio P.L.,
Martorana V.,
Emanuele A.,
Vaiana S.M.,
Manno M.,
Bulone D.,
PalmaVittorelli M.B.,
Palma M.U.
Publication year - 1999
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19991001)37:1<116::aid-prot11>3.0.co;2-i
Subject(s) - coagulation , chemistry , biophysics , protein aggregation , conformational change , amyloidosis , fibril , amyloid (mycology) , biochemistry , biology , medicine , pathology , inorganic chemistry , psychiatry
A strong interest is currently focused on protein self‐association and deposit. This usually involves conformational changes of the entire protein or of a fragment. It can occur even at low concentrations and is responsible for pathologies such as systemic amyloidosis, Alzheimer's and Prion diseases, and other neurodegenerative pathologies. Readily available proteins, exhibiting at low concentration self‐association properties related to conformational changes, offer very convenient model systems capable of providing insight into this class of problems. Here we report experiments on bovine serum albumin, showing that the process of conformational change of this protein towards an intermediate form required for coagulation occurs simultaneously and interacts with two more processes: mesoscopic demixing of the solution and protein cross‐linking. This pathway of three interacting processes allows coagulation even at very low concentrations, and it has been recently observed also in the case of a nonpeptidic polymer. It could therefore be a fairly common feature in polymer coagulation/gelation. Proteins 1999;37: 116–120. © 1999 Wiley‐Liss, Inc.