Two‐Dimensional Ultraviolet (2DUV) Spectroscopic Tools for Identifying Fibrillation Propensity of Protein Residue Sequences | Zendy

Jiang Jun | Zendy; Mukamel Shaul | Zendy

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Two‐Dimensional Ultraviolet (2DUV) Spectroscopic Tools for Identifying Fibrillation Propensity of Protein Residue Sequences

Author(s) -

Jiang Jun,

Mukamel Shaul

Publication year - 2010

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201005093

Subject(s) - ultraviolet , fibril , chemistry , amyloid fibril , spectroscopy , residue (chemistry) , crystallography , fibrillation , ultraviolet visible spectroscopy , biophysics , materials science , biochemistry , biology , physics , amyloid β , organic chemistry , medicine , optoelectronics , disease , quantum mechanics , atrial fibrillation , pathology , cardiology

Distinctive feature : Two‐dimensional ultraviolet (2DUV) spectroscopy can be utilized to identify protein sequences capable of forming fibrils. The Rosetta free energy of proteins, which is a good indicator of fibrillation propensity, has distinct 2DUV signatures. An additional positive diagonal peak at 54 000–58 000 cm −1 in chiral xxxy spectra serves as a indicator of the ability of protein sequences to form amyloid‐like fibrils.

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