Ladungsinduziertes Entwinden isolierter Proteine zu einer definierten Sekundärstruktur

Abstract

In einer kombinierten experimentellen und theoretischen Studie untersuchen wir die Sekundärstruktur isolierter Proteine in Abhängigkeit ihrer Ladung. In den Infrarotspektren der Proteine Ubiquitin und Cytochromc treten Amid-I-

IR spectroscopy of protonated leu-enkephalin and its 18-crown-6 complex embedded in helium droplets

“…It provides spectra of very cold molecules, does not require the presence of a chromophore, has a rather weak interaction with the helium solvation shell, and can be extended to large species. 34…”

Infrared Multiphoton Dissociation Spectroscopy with Free‐Electron Lasers: On the Road from Small Molecules to Biomolecules

“…IRMPD spectroscopy is useful to detect the characteristic protein bands of amide I (usually at approximately 1650 cm −1 ; C=O stretching) and amide II (usually at approximately 1550 cm −1 ; N−H bending). These bands serve as spectral markers of the helical structure of proteins …”

“…IRMPD spectroscopy was used to determine the secondary structure of multiply protonated ubiquitin and cytochrome c (Figure ) . The IRPMD spectra of both biomolecules at low and intermediate charge states (denoted by L and I in Figure ) show the typical amide I and II bands.…”

“…Gray trace segments for ubiquitin 10+ and 11+ denote a higher photon density. Three types of bands identified are labelled amide IIa, amide IIb, and amide I. Reprinted from reference .…”