Peptide-Induced Amyloid-Like Conformational Transitions in Proteins
Author(s) -
Egorov Vv,
Н. А. Грудинина,
Andrey V. Vasin,
Д. В. Лебедев
Publication year - 2015
Publication title -
international journal of peptides
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.239
H-Index - 25
eISSN - 1687-9775
pISSN - 1687-9767
DOI - 10.1155/2015/723186
Subject(s) - conformational change , amyloid (mycology) , protein structure , chemistry , protein folding , biophysics , biochemistry , microbiology and biotechnology , biology , inorganic chemistry
Changes in protein conformation can occur both as part of normal protein functioning and during disease pathogenesis. The most common conformational diseases are amyloidoses. Sometimes the development of a number of diseases which are not traditionally related to amyloidoses is associated with amyloid-like conformational transitions of proteins. Also, amyloid-like aggregates take part in normal physiological processes such as memorization and cell signaling. Several primary structural features of a protein are involved in conformational transitions. Also the protein proteolytic fragments can cause the conformational transitions in the protein. Short peptides which could be produced during the protein life cycle or which are encoded by short open reading frames can affect the protein conformation and function.
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