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Int. J. Mol. Sci. 2014, 15(5), 8428-8442; doi:10.3390/ijms15058428
Article

Access of Hydrogen-Radicals to the Peptide-Backbone as a Measure for Estimating the Flexibility of Proteins Using Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry

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Received: 12 March 2014; in revised form: 11 April 2014 / Accepted: 30 April 2014 / Published: 13 May 2014
(This article belongs to the Special Issue Mass Spectrometry Application in Biology)
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Abstract: A factor for estimating the flexibility of proteins is described that uses a cleavage method of “in-source decay (ISD)” coupled with matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS). The MALDI-ISD spectra of bovine serum albumin (BSA), myoglobin and thioredoxin show discontinuous intense ion peaks originating from one-side preferential cleavage at the N-Cα bond of Xxx-Asp, Xxx-Asn, Xxx-Cys and Gly-Xxx residues. Consistent with these observations, Asp, Asn and Gly residues are also identified by other flexibility measures such as B-factor, turn preference, protection and fluorescence decay factors, while Asp, Asn, Cys and Gly residues are identified by turn preference factor based on X-ray crystallography. The results suggest that protein molecules embedded in/on MALDI matrix crystals partly maintain α-helix and that the reason some of the residues are more susceptible to ISD (Asp, Asn, Cys and Gly) and others less so (Ile and Val) is because of accessibility of the peptide backbone to hydrogen-radicals from matrix molecules. The hydrogen-radical accessibility in MALDI-ISD could therefore be adopted as a factor for measuring protein flexibility.
Keywords: proteins; hydrogen-radical; flexibility; MALDI MS (matrix-assisted laser desorption/ionization mass spectrometry); in-source decay proteins; hydrogen-radical; flexibility; MALDI MS (matrix-assisted laser desorption/ionization mass spectrometry); in-source decay
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

Takayama, M.; Nagoshi, K.; Iimuro, R.; Inatomi, K. Access of Hydrogen-Radicals to the Peptide-Backbone as a Measure for Estimating the Flexibility of Proteins Using Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry. Int. J. Mol. Sci. 2014, 15, 8428-8442.

AMA Style

Takayama M, Nagoshi K, Iimuro R, Inatomi K. Access of Hydrogen-Radicals to the Peptide-Backbone as a Measure for Estimating the Flexibility of Proteins Using Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry. International Journal of Molecular Sciences. 2014; 15(5):8428-8442.

Chicago/Turabian Style

Takayama, Mitsuo; Nagoshi, Keishiro; Iimuro, Ryunosuke; Inatomi, Kazuma. 2014. "Access of Hydrogen-Radicals to the Peptide-Backbone as a Measure for Estimating the Flexibility of Proteins Using Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry." Int. J. Mol. Sci. 15, no. 5: 8428-8442.


Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert