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Intrinsic folding of the cysteine residue: competition between folded and extended forms mediated by the -SH group

Phys Chem Chem Phys. 2020; 
Gildas Goldsztejn, Venkateswara Rao Mundlapati, Valérie Brenner, Eric Gloaguen, Michel Mons, Carlos Cabezas, Iker León, José Luis Alonso
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Molecular Biology Reagents … Z-Cys-NH 2 (Genscript) was mixed with graphite (1 : 4 molecular weight ratio) and pressed a into 6 mm pellet, fixed close to the 1 mm diameter nozzle of a pulsed valve, operating with a 30 : 70 He : Ne mixture at a backing pressure of 18 bars … Get A Quote

摘要

A dual microwave and optical spectroscopic study of a capped cysteine amino acid isolated in a supersonic expansion, combined with quantum chemistry modelling, enabled us to characterize the conformational preferences of Cys embedded in a protein chain. IR/UV double resonance spectroscopy provided evidence for the coexistence of two conformers, assigned to folded and extended backbones (with classical C7 and C5 backbone H-bonding respectively), each of them additionally stabilized by specific main-chain/side-chain H-bonding, where the sulfur atom essentially plays the role of H-bond acceptor. The folded structure was confirmed by microwave spectroscopy, which demonstrated the validity of the DFT-D methods curre... More

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