Literature DB >> 2804067

Evaluation of the secondary structure of apo B-100 in low-density lipoprotein (LDL) by infrared spectroscopy.

E Goormaghtigh1, J De Meutter, B Vanloo, R Brasseur, M Rosseneu, J M Ruysschaert.   

Abstract

The secondary structure of the apo B-100 protein present in human low density lipoprotein has been investigated by transmission and attenuated total reflection infrared spectroscopy. The amount of beta-sheet (41%) is significantly higher than that determined by CD spectroscopy in the present study (12%) and elsewhere (15-16%). The high percentage of beta-sheet structure in apo B-100 supports the importance of such segments in maintaining the lipid-protein assembly in LDL. Polarized infrared spectroscopy indicates that the beta-sheet component of apo B-100 adopts a preferential orientation with respect to the phospholipid monolayer surrounding the LDL, whereas no such orientation is observed for the other secondary structure components.

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Year:  1989        PMID： 2804067     DOI： 10.1016/0005-2760(89)90338-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  9 in total

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7.  Structure and orientation of apo B-100 peptides into a lipid bilayer.

Authors:  L Lins; R Brasseur; M Rosseneu; C Y Yang; D A Sparrow; J T Sparrow; A M Gotto; J M Ruysschaert
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8.  Evaluation of protein secondary structure from FTIR spectra improved after partial deuteration.

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  9 in total

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