Investigation of membrane penetration depth and interactions of the amino-terminal domain of huntingtin: refined analysis by tryptophan fluorescence measurement-Reference-Cited by-同舟云学术

Investigation of membrane penetration depth and interactions of the amino-terminal domain of huntingtin: refined analysis by tryptophan fluorescence measurement

Published:2014-06-04 Issue:8-9 Volume:43 Page:347-360
ISSN:0175-7571
Container-title:European Biophysics Journal
language:en
Short-container-title:Eur Biophys J

Author:

Michalek Matthias,Aisenbrey Christopher,Bechinger Burkhard

Publisher

Springer Science and Business Media LLC

Subject

General Medicine,Biophysics

Link

http://link.springer.com/content/pdf/10.1007/s00249-014-0966-9.pdf

Reference39 articles.

1. Aisenbrey C, Bechinger B, Grobner G (2008) Macromolecular crowding at membrane interfaces: adsorption and alignment of membrane peptides. J Mol Biol 375:376–385

2. Atwal RS, Xia J, Pinchev D, Taylor J, Epand RM, Truant R (2007) Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum Mol Genet 16:2600–2615

3. Bechinger B, Kinder R, Helmle M, Vogt TC, Harzer U, Schinzel S (1999) Peptide structural analysis by solid-state NMR spectroscopy. Biopolymers 51:174–190

4. Bechinger B, Aisenbrey C, Bertani P (2004) The alignment, structure and dynamics of membrane-associated polypeptides by solid-state NMR spectroscopy. Biochim Biophys Acta 1666:190–204

5. Bolen EJ, Holloway PW (1990) Quenching of tryptophan fluorescence by brominated phospholipid. Biochemistry 29:9638–9643

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