Gas-phase conformations of proteolytically derived protein fragments: Influence of solvent on peptide conformation

被引:26
作者
Ruotolo, BT [1 ]
Russell, DH [1 ]
机构
[1] Texas A&M Univ, Dept Chem, Lab Biol Mass Spectrometry, College Stn, TX 77843 USA
关键词
D O I
10.1021/jp0490296
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The structures of 4 tryptic peptides are studied using matrix-assisted laser desorption ionization-ion mobility mass spectrometry, circular dichroism spectroscopy, and solution-phase hydrogen-deuterium exchange mass spectrometry. The sequences LLGNVLVVVLAR (bovine hemoglobin) and HGTVVLTALGGILK (horse heart myoglobin) are helical within their native proteins and as gas-phase ions [J. Am. Chem. Soc. 2002, 124, 4214]; however, the two peptides undergo very different structural transitions as their local environment is changed. For example, circular dichroism measurements suggest that the peptide LLGNVLVVVLAR assumes a beta-hairpin conformation in aqueous/methanolic solvent systems; however, the helical structure of HGTVVLTALGGILK appears to be denatured (takes on a random coil conformation) upon cleavage from the protein. The gas-phase structure of the peptides exhibit a high correlation to the conformation observed by circular dichroism in 2,2,2-trifluoroethanol, suggesting that the gas-phase structure may be utilized for solution-phase relevant studies of peptide folding.
引用
收藏
页码:15321 / 15331
页数:11
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