Apomyoglobin forms a micellar complex with phospholipid at low pH
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(88)81056-1/fullpdf
Reference17 articles.
1. A Review of Plasma Apolipoprotein A-I Interactions with Phosphatidylcholines
2. Size and shape of the model lipoprotein complex formed between glucagon and dimyristoylglycerophosphocholine
3. Amphipathic helix and its relationship to the interaction of calcitonin with phospholipids
4. Morphological changes of phosphatidylcholine bilayers induced by melittin: vesicularization, fusion, discoidal particles
5. Interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles. I. A microcalorimetric and fluorescence study
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1. Model phospholipid membranes affect the tertiary structure of holomyoglobin: Conformational changes at pH 6.2;Molecular Biology;2005-01
2. Highly deiminated isoform of myelin basic protein from multiple sclerosis brain causes fragmentation of lipid vesicles;Journal of Neuroscience Research;1999-08-15
3. The structural homology between uteroglobin and the pore-forming domain of colicin A suggests a possible mechanism of action for uteroglobin;Protein Science;1996-05
4. Fragmentation of dimyristoylphosphatidylcholine vesicles by apomyoglobin;Archives of Biochemistry and Biophysics;1992-09
5. pH-Dependent membrane fusion and vesiculation of phospholipid large unilamellar vesicles induced by amphiphilic anionic and cationic peptides;Biochemistry;1992-02
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