13C NMR evidence that substitution of glutamine for arginine 3500 in familial defective apolipoprotein B-100 disrupts the conformation of the receptor-binding domain.
Open Access
- 1 February 1991
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (5) , 2701-2704
- https://doi.org/10.1016/s0021-9258(18)49900-0
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Evaluation of the secondary structure of apo B-100 in low-density lipoprotein (LDL) by infrared spectroscopyPublished by Elsevier ,2003
- Familial defective apolipoprotein B-100: low density lipoproteins with abnormal receptor binding.Proceedings of the National Academy of Sciences, 1987
- Sequence, structure, receptor-binding domains and internal repeats of human apolipoprotein B-100Nature, 1986
- Complete protein sequence and identification of structural domains of human apolipoprotein BNature, 1986
- Packing of cholesterol molecules in human low-density lipoproteinBiochemistry, 1986
- A Receptor-Mediated Pathway for Cholesterol HomeostasisScience, 1986
- [28] Nuclear magnetic resonance studies of lipoproteinsPublished by Elsevier ,1986
- Human Apolipoprotein B: Structure of Carboxyl-Terminal Domains, Sites of Gene Expression, and Chromosomal LocalizationScience, 1985
- Mechanism of dissociation of human apolipoproteins A-I, A-II, and C from complexes with dimyristoylphosphatidylcholine as studied by thermal denaturationBiochemistry, 1984
- [50] Protein labeling by reductive alkylationPublished by Elsevier ,1983