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Cover Picture: Structural Insights into the Trp‐Cage Folding Intermediate Formation (Chem. Eur. J. 8/2013)
Author(s) -
Rovó Petra,
Stráner Pál,
Láng András,
Bartha István,
Huszár Kristóf,
Nyitray László,
Perczel András
Publication year - 2013
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201390021
Subject(s) - chemistry , crystallography , supramolecular chemistry , isomerization , energy landscape , stereochemistry , thiophene , folding (dsp implementation) , molecule , catalysis , crystal structure , organic chemistry , biochemistry , electrical engineering , engineering
The folding energy landscape of the smallest protein, the 20‐residue long Trp‐cage, is more rugged than expected. Temperature‐dependent NMR measurements revealed that at neutral pH the final step of the Trp‐cage folding is a fast secondary structural rearrangement: the short α‐helical G 11 –G 15 segment of the intermediate (I) converts into a 3 10 ‐helix and thus, the polypeptide adopts the most stable, folded (F) structure. At acidic pH the isomerization of the G 11 P 12 peptide bond slows down the folding process: two off‐pathway intermediate unfolded states (U′ and U′′) emerge. These two states have no native‐like structure and show elevated internal mobility. For more information see the Full Paper by A. Perczel et al. on page 2628 ff.