External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of proteins at low concentrations View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-12

AUTHORS

Andreas Schwaighofer, Mirta R Alcaráz, Can Araman, Héctor Goicoechea, Bernhard Lendl

ABSTRACT

Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy are analytical techniques employed for the analysis of protein secondary structure. The use of CD spectroscopy is limited to low protein concentrations (<2 mg ml(-1)), while FTIR spectroscopy is commonly used in a higher concentration range (>5 mg ml(-1)). Here we introduce a quantum cascade laser (QCL)-based IR transmission setup for analysis of protein and polypeptide secondary structure at concentrations as low as 0.25 mg ml(-1) in deuterated buffer solution. We present dynamic QCL-IR spectra of the temperature-induced α-helix to β-sheet transition of poly-L-lysine. The concentration dependence of the α-β transition temperature between 0.25 and 10 mg ml(-1) was investigated by QCL-IR, FTIR and CD spectroscopy. By using QCL-IR spectroscopy it is possible to perform IR spectroscopic analysis in the same concentration range as CD spectroscopy, thus enabling a combined analysis of biomolecules secondary structure by CD and IR spectroscopy. More... »

PAGES

33556

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep33556

DOI

http://dx.doi.org/10.1038/srep33556

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045455929

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27633337


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