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  Analyzing heat capacity profiles of peptide-containing membranes: Cluster formation of gramicidin A

Ivanova, V. P., Makarov, I., Schaeffer, T. E., & Heimburg, T. (2003). Analyzing heat capacity profiles of peptide-containing membranes: Cluster formation of gramicidin A. Biophysical Journal, 84(4), 2427-2439. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B94RW-4V40XMW-10-1&_cdi=56421&_user=38661&_pii=S0006349503750474&_orig=search&_coverDate=04%2F30%2F2003&_sk=999159995&view=c&wchp=dGLzVtz-zSkWA&md5=d2b174cffa19f23dbbb4d799e8982cf1&ie=/sdarticle.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F136-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-EC09-1
Genre: Journal Article

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 Creators:
Ivanova, V. P.1, Author              
Makarov, I., Author
Schaeffer, T. E.2, Author              
Heimburg, T.1, Author              
Affiliations:
1Research Group of Biophysics and Thermodynamics of Membranes, MPI for biophysical chemistry, Max Planck Society, ou_578546              
2Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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 Abstract: The analysis of peptide and protein partitioning in lipid membranes is of high relevance for the understanding of biomembrane function. We used statistical thermodynamics analysis to demonstrate the effect of peptide mixing behavior on heat capacity profiles of lipid membranes with the aim to predict peptide aggregation from cP-profiles. This analysis was applied to interpret calorimetric data on the interaction of the antibiotic peptide gramicidin A with lipid membranes. The shape of the heat capacity profiles was found to be consistent with peptide clustering in both gel and fluid phase. Applying atomic force microscopy, we found gramicidin A aggregates and established a close link between thermodynamics data and microscopic imaging. On the basis of these findings we described the effect of proteins on local fluctuations. It is shown that the elastic properties of the membrane are influenced in the peptide environment.

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Language(s): eng - English
 Dates: 2005-08-162003-04
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 84 (4) Sequence Number: - Start / End Page: 2427 - 2439 Identifier: -