Sökning: WFRF:(Song Henry) >
The amide I spectru...
The amide I spectrum of parallel β-sheet proteins
-
- Baronio, Cesare M. (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
- Li, Huimin (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
- Song, Guangyuan (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
visa fler...
-
- Annecke, Henry (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
- Gustafsson, Robert (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
- Martinez-Carranza, Markel (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
- Stenmark, Pål (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
- Barth, Andreas (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik
-
visa färre...
-
(creator_code:org_t)
- Engelska.
- Relaterad länk:
-
https://su.diva-port... (primary) (Raw object)
-
visa fler...
-
https://urn.kb.se/re...
-
visa färre...
Abstract
Ämnesord
Stäng
- The amide I absorption of the polypeptide backbone has long been used to analyze the secondary structure of proteins. This approach has gained additional attention in the context of amyloid diseases where a particular focus is on the distinction between parallel and antiparallel β-sheets because these structures often discriminate between pre-fibrillar structures and fibrils. Some earlier infrared spectra with typical features of antiparallel β-sheets were interpreted as arising from the parallel β-sheets of fibrils. Therefore, the ability of infrared spectroscopy to distinguish between both types of β-sheets is debated. While it is established that regular, antiparallel β-sheets give rise to a high wavenumber band near 1690 cm-1, it is less clear whether or not this band may also occur for parallel β-sheets. Here we present and analyze the amide I spectra of two β-helix proteins, SV2 and Pent. The overall shape of the proteins is that of a cuboid which has parallel β-sheets on its four sides, which are connected by bends. The main features of their amide I spectrum are a band at 1665, and two bands between 1645 and 1628 cm-1. Both proteins exhibit also a weak component band near 1690 cm-1. Calculations of the amide I spectrum indicate that the absorption at high wavenumbers is not caused by the parallel β-sheets but by the bends between the β-strands. We therefore suggest to modify the interpretation of the amide I spectrum as follows: a high wavenumber band near 1690 cm-1 may be caused by other structures than antiparallel β-sheets. However, when the spectrum consists of only two distinct bands, one near 1690 cm-1 and one near 1630 cm-1, then an assignment to antiparallel β-sheets is consistent with the literature.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Nyckelord
- Biophysics
- biofysik
Publikations- och innehållstyp
- vet (ämneskategori)
- ovr (ämneskategori)