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Towards gelsolin amyloid formation
Author(s) -
Liepina Inta,
Janmey Paul,
Czaplewski Cezary,
Liwo Adam
Publication year - 2004
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20175
Subject(s) - gelsolin , amyloid fibril , chemistry , amyloid (mycology) , fibril , hydrogen bond , biophysics , molecular dynamics , protein aggregation , amyloid β , crystallography , biochemistry , actin , molecule , computational chemistry , organic chemistry , medicine , inorganic chemistry , disease , pathology , biology
Amyloid diseases result from protein misfolding and aggregation into fibrils. Some features of gelsolin amyloidogenic fragments comprised of residues 173–243 (G173–243) and residues 173–202 (G173–202) were investigated by the method of molecular dynamics (MD). The α‐helical structure of G173–243 present in the whole protein unwinds during the course of MD simulation of the fragment G173–243, suggesting that the G173–243 structure is not stable and could unfold before becoming involved in gelsolin amyloid fibril formation. Twelve fragments of G173–202 were used to build a possible β‐fibril. During the course of the simulation, G173–202 fragments formed hydrogen bonds and tended to turn by an angle of 10°–20° towards each other. © 2004 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2004