Advanced approaches for the characterization of a de novo designed antiparallel coiled coil peptide.

Content Provider	Semantic Scholar
Author	Pagel, Kevin Seeger, Karsten Seiwert, Bettina Villa, Alessandra Mark, Alan E. Berger, Stefan Koksch, Beate
Copyright Year	2005
Abstract	We report here an advanced approach for the characterization of the folding pattern of a de novo designed antiparallel coiled coil peptide by high-resolution methods. Incorporation of two fluorescence labels at the C- and N-terminus of the peptide chain as well as modification of two hydrophobic core positions by Phe/[15N,13C]Leu enable the study of the folding characteristics and of distinct amino acid side chain interactions by fluorescence resonance energy transfer (FRET) and NMR spectroscopy. Results of both experiments reveal the antiparallel alignment of the helices and thus prove the design concept. This finding is also supported by molecular dynamics simulations. Electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry (ESI-FTICR-MS) in combination with NMR experiments was used for verification of the oligomerization equilibria of the coiled coil peptide.
Starting Page	943
Ending Page	947
Page Count	5
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://compbio.biosci.uq.edu.au/mediawiki/upload/4/4a/AM_05_05.pdf
PubMed reference number	15785806v1
Volume Number	3
Issue Number	7
Journal	Organic & biomolecular chemistry
Language	English
Access Restriction	Open
Subject Keyword	Alignment Amino Acids Biomedicine Charge (electrical) Coil Device Component Coiled-Coil Domain Cyclotrons Financial Statements Fluorescence Resonance Energy Transfer Ions Magnetic Resonance Imaging Molecular Dynamics Spectrometry Spectrometry, Mass, Electrospray Ionization Spectroscopy, Nuclear Magnetic Resonance Thioctic Acid Transfer RNA Aminoacylation Verification of Theories
Content Type	Text
Resource Type	Article