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Literature DB >> 8507644

Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy.

E Goormaghtigh¹, V Cabiaux, J De Meutter, M Rosseneu, J M Ruysschaert.

Abstract

The secondary structure of the human low-density lipoprotein (LDL) apo B-100 fragment embedded in the lipid domain of the particle has been investigated by Fourier transform attenuated total reflection infrared spectroscopy (FTIR-ATR). The solvent-exposed region of the protein was hydrolyzed by using different proteases (alpha-chymotrypsin, trypsin, proteinase K) for incubation times varying between 24 min and 48 h. Analysis of the FTIR-ATR spectra after repurification of the digested LDL particle indicates the same trend for all the hydrolysis conditions tested: the peptides remaining associated with the particle are rich in beta-sheet structure. Dichroism spectra reveal that at least part of the beta-sheets is associated with the phospholipid component of the particle.

Entities: Chemical Gene Species

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Year: 1993 PMID： 8507644 DOI： 10.1021/bi00074a023

Source DB: PubMed Journal: Biochemistry ISSN： 0006-2960 Impact factor: 3.162

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Cited

7 in total

1. Three-dimensional structure of low density lipoproteins by electron cryomicroscopy.

Authors: E V Orlova; M B Sherman; W Chiu; H Mowri; L C Smith; A M Gotto
Journal: Proc Natl Acad Sci U S A Date: 1999-07-20 Impact factor: 11.205

2. Quantitative determination of low density lipoprotein oxidation by FTIR and chemometric analysis.

Authors: Henry S Lam; Andrew Proctor; John Nyalala; Manford D Morris; W Grady Smith
Journal: Lipids Date: 2004-07 Impact factor: 1.880

3. Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: an infrared spectroscopy study.

Authors: I Martin; M C Dubois; F Defrise-Quertain; T Saermark; A Burny; R Brasseur; J M Ruysschaert
Journal: J Virol Date: 1994-02 Impact factor: 5.103

7. Structural analysis of APOB variants, p.(Arg3527Gln), p.(Arg1164Thr) and p.(Gln4494del), causing Familial Hypercholesterolaemia provides novel insights into variant pathogenicity.

Authors: J A Fernández-Higuero; A Etxebarria; A Benito-Vicente; A C Alves; J L R Arrondo; H Ostolaza; M Bourbon; C Martin
Journal: Sci Rep Date: 2015-12-08 Impact factor: 4.379

7 in total

Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy.

1. Three-dimensional structure of low density lipoproteins by electron cryomicroscopy.

2. Quantitative determination of low density lipoprotein oxidation by FTIR and chemometric analysis.

3. Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: an infrared spectroscopy study.

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

5. Structural changes induced by acidic pH in human apolipoprotein B-100.

6. Human LDL structural diversity studied by IR spectroscopy.

7. Structural analysis of APOB variants, p.(Arg3527Gln), p.(Arg1164Thr) and p.(Gln4494del), causing Familial Hypercholesterolaemia provides novel insights into variant pathogenicity.