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The variation of the gas phase acidity of a cysteine residue in oligopeptides

Author

Jialin Shen, University of the Pacific

Date of Award

2011

Document Type

Thesis - Pacific Access Restricted

Degree Name

Master of Science (M.S.)

Department

Chemistry

First Advisor

Jianhua Ren

First Committee Member

Patrick R. Jones

Second Committee Member

Mike McCallum

Abstract

The altered acidities of amino acid residues in folded proteins can be used as a good indication for the diverse functions, stabilities as well as folding-unfolding states of the proteins. Previously, our group has investigated the gas phase acidities of a series of cysteine containing peptides of four residues and longer. The results showed that the helix macrodipole might have a significant influence on the acidities of these peptides. In this work, the gas phase acidities of isomeric small cysteine containing di- and tri-peptides were investigated experimentally and computationally.

The gas phase acidities (Δ_acidG) and related thermochemical quantities (Δ_acidH and Δ_acidS) were determined by using the extended Cooks kinetic method. A triple-quadruple mass spectrometer interfaced with an electrospray ionization source was employed for the study. The gas phase acidities of the N-terminal cysteine peptides (CysAla_1,2NH₂ and CysGly_1,2NH₂) were determined to be in the range of 321-323 kcal/mol, and the acidities of the C-terminal cysteine peptides (Ala_1,2CysNH₂ and Gly_1,2CysNH₂) were around 327- 331 kcal/mol. The results showed that theN-cysteine peptides were more acidic than the corresponding C-cysteine peptides, tri-peptides were stronger acids than di-peptides, and the acidities of cysteine-polyglycine peptides were close to those of the cysteine-polyalanine analogues.

Computational studies were performed through conformer search, geometry optimization, and energy calculations using the Spartan and the Gaussian suite of programs. The results showed that the low energy conformations of all deprotonated peptides were coils. The greater acidities of the N-cysteine peptides were likely due to the stronger hydrogen-bonding interactions in the deprotonated N-cysteine peptides, which efficiently stabilized the thiolate anions. The theoretically predicted acidities were in good agreements with the experimental results.

Pages

123

Recommended Citation

Shen, Jialin. (2011). The variation of the gas phase acidity of a cysteine residue in oligopeptides. University of the Pacific, Thesis - Pacific Access Restricted. https://scholarlycommons.pacific.edu/uop_etds/791