期刊
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
卷 17, 期 3, 页码 2169-2178出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4cp04449e
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资金
- Fondation de Cooperation Scientifique Campus Paris-Saclay, through the Inter-Labex PALM-CHARMMMAT - French National Research Agency [LALIFOLD2013-0272I, ANR-11-IDEX-0003-02]
Intra-residue interactions play an important role in proteins by influencing local folding of the backbone. Taking advantage of the capability of gas phase experiments to provide relevant information on the intrinsic H-bonding pattern of isolated peptide chains, the intra-residue interactions of serine and cysteine residues, i.e., OH/SH center dot center dot center dot OC(i) C6 and NH(i)center dot center dot center dot O/S C5 interactions in Ser/Cys residues, are probed by laser spectroscopy of isolated peptides. The strength of these local side chain-main chain interactions, elegantly documented from their IR spectral features for well-defined conformations of the main chain, demonstrates that a subtle competition exists between the two types of intra-residue bond: the C6 H-bond is the major interaction with Ser, in contrast to Cys where C5 interaction takes over. The restricted number of conformers observed in the gas phase experiment with Ser compared to Cys (where both extended and folded forms are observed) also suggests a significant mediation role of these intra-residue interactions on the competition between the several main chain folding patterns.
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