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Back Cover: Aromatic Cluster Sensor of Protein Folding: Near‐UV Electronic Circular Dichroism Bands Assigned to Fold Compactness (Chem. Eur. J. 39/2016)
Author(s) -
Farkas Viktor,
Jákli Imre,
Tóth Gábor K.,
Perczel András
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201603201
Subject(s) - circular dichroism , chemistry , crystallography , protein folding , folding (dsp implementation) , biochemistry , engineering , electrical engineering
As in Trp‐cages derived from Exenatide , other proteins of important biological relevance also have Trp↔Tyr interacting core residues giving rise to 3D‐fold characteristic chiroptical properties: Electronic circular dichroism (ECD) data combined with suitable deconvolution methods (e.g., CCA+) were used. The NMR cross‐validated ensemble of (mini)proteins show that 1) both L b 280 and L b 293 bands report 3D‐structure compactness and 2) for the first time, the pure near‐UV ECD spectrum of the unfolded state is described. More information can be found in the Full Paper by A. Perczel et al. on page 13871 ff.