期刊
JOURNAL OF CHEMICAL THEORY AND COMPUTATION
卷 12, 期 3, 页码 930-934出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jctc.5b01114
关键词
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资金
- Fundacao para a Ciencia e a Tecnologia [SFRH/BD/81017/2011, PTDC/QUI-BIQ/113721/2009, ULD/MULTI/00612/2013, PTDC/QEQCOM/5904/2014]
- Fundação para a Ciência e a Tecnologia [PTDC/QUI-BIQ/113721/2009, SFRH/BD/81017/2011] Funding Source: FCT
Peptides and proteins protonation equilibrium is strongly influenced by its surrounding media. Remarkably, until now, there have been no quantitative and systematic studies reporting the pK(a) shifts in the common titrable amino acids upon lipid membrane insertion. Here, we applied our recently developed CpHMD-L method to calculate the pK(a) values of titrable amino acid residues incorporated in Ala-based pentapeptides at the water/membrane interface. We observed that membrane insertion leads to desolvation and a clear stabilization of the neutral forms, and we quantified the increases/decreases of the pK(a) values in the anionic/cationic residues along the membrane normal. This work highlights the importance of properly modeling the protonation equilibrium in peptides and proteins interacting with membranes using molecular dynamics simulations.
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