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Plos One : Role of the N-terminal Seven Residues of Surfactant Protein B Sp-b, Volume 8

By Massiah, Michael

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Book Id: WPLBN0003966274
Format Type: PDF eBook :
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Reproduction Date: 2015

Title: Plos One : Role of the N-terminal Seven Residues of Surfactant Protein B Sp-b, Volume 8  
Author: Massiah, Michael
Volume: Volume 8
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Historic
Publication Date:
Publisher: Plos

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Massiah, M. (n.d.). Plos One : Role of the N-terminal Seven Residues of Surfactant Protein B Sp-b, Volume 8. Retrieved from http://netlibrary.net/


Description
Description : Breathing is enabled by lung surfactant, a mixture of proteins and lipids that forms a surface-active layer and reduces surface tension at the air-water interface in lungs. Surfactant protein B (SP-B) is an essential component of lung surfactant. In this study we probe the mechanism underlying the important functional contributions made by the N-terminal 7 residues of SP-B, a region sometimes called the ‘‘insertion sequence’’. These studies employed a construct of SP-B, SP-B (1–25,63–78), also called Super Mini-B, which is a 41-residue peptide with internal disulfide bonds comprising the N-terminal 7-residue insertion sequence and the N- and C-terminal helices of SP-B. Circular dichroism, solution NMR, and solid state 2H NMR were used to study the structure of SP-B (1–25,63–78) and its interactions with phospholipid bilayers. Comparison of results for SP-B (8–25,63–78) and SP-B (1–25,63–78) demonstrates that the presence of the 7-residue insertion sequence induces substantial disorder near the centre of the lipid bilayer, but without a major disruption of the overall mechanical orientation of the bilayers. This observation suggests the insertion sequence is unlikely to penetrate deeply into the bilayer. The 7- residue insertion sequence substantially increases the solution NMR linewidths, most likely due to an increase in global dynamics.

 

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