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Determination of amyloid core structure using chemical shifts
Author(s) -
Skora Lukasz,
Zweckstetter Markus
Publication year - 2012
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2170
Subject(s) - fibril , amyloid fibril , amyloid (mycology) , biophysics , chemistry , characterization (materials science) , core (optical fiber) , amyloid disease , protein structure , amyloid β , crystallography , materials science , biochemistry , nanotechnology , biology , pathology , medicine , disease , composite material , inorganic chemistry
Amyloid fibrils are the pathological hallmark of a large variety of neurodegenerative disorders. The structural characterization of amyloid fibrils, however, is challenging due to their non‐crystalline, heterogeneous, and often dynamic nature. Thus, the structure of amyloid fibrils of many proteins is still unknown. We here show that the structure calculation program CS‐Rosetta can be used to obtain insight into the core structure of amyloid fibrils. Driven by experimental solid‐state NMR chemical shifts and taking into account the polymeric nature of fibrils CS‐Rosetta allows modeling of the core of amyloid fibrils. Application to the Y145X stop mutant of the human prion protein reveals a left‐handed β‐helix