In the early 1970s, the existence of a "lipid annulus" stably surrounding the individual intrinsic protein molecules was proposed by several authors. They referred to a number of lipid molecules in slow exchange with the bulk lipid in the bilayer, i.e., more or less protein-bound, and more ordered than the bulk lipid. The annular lipids would control enzyme activity. This idea was uncritically accepted by most scientists working with intrinsic membrane proteins at the time, so that the idea operated like a myth in the field. However, in the following decade, hard spectroscopic and biochemical evidence showed that the proposed annular lipids were not immobilized for a sufficiently long time to influence enzyme or transporter activity, nor were they ordered by the protein. Surprisingly, forty years later, the myth survives, and the term 'annular lipid' is still in use, in a different, but even more illogical sense.
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http://dx.doi.org/10.3390/biomedicines10112672 | DOI Listing |
Skinmed
January 2025
Department of Dermatology, Faculty of Medicine, Jordan University of Science and Technology, Irbid, Jordan.
A 53-year-old woman presented with an eruption on her face and body for 2 weeks that had developed first on the face before spreading to the trunk and extremities. There was burning with sunlight exposure. Her medical conditions included diabetes mellitus, vitamin D deficiency, and hyperlipidemia.
View Article and Find Full Text PDFJ Phys Chem Lett
January 2025
Department of Chemistry, IIT Jodhpur, Jodhpur, Rajasthan 342037, India.
The plant thylakoid membrane hosting the light-harvesting complex (LHCII) is the site of oxygenic photosynthesis. Contrary to the earlier consensus of a protein-driven single lamellar phase of the thylakoid, despite containing 40% non-bilayer-forming lipids, recent experiments confirm the polymorphic state of the functional thylakoid. What, then, is the origin of this polymorphism and what factors control it? The current Letter addresses the question using a total of 617.
View Article and Find Full Text PDFFront Mol Biosci
November 2024
Institut de Biologie Structurale J.-P. Ebel, Université Grenoble Alpes-CEA-CNRS, Grenoble, France.
The primary goal of our work is to provide structural insights into the influence of the hydrophobic lipid environment on the membrane proteins (MPs) structure and function. Our work will not cover the well-studied hydrophobic mismatch between the lipid bilayer and MPs. Instead, we will focus on the less-studied direct molecular interactions of lipids with the hydrophobic surfaces of MPs.
View Article and Find Full Text PDFFoods
October 2024
Leibniz Institute for Food Systems Biology at the Technical University of Munich, Lise-Meitner-Str. 34, 85354 Freising, Germany.
Functional amyloids (protein nanofibrils, PNF) synthesized from plant sources exhibit unique physicochemical and nanomechanical properties that could improve food texture. While environmental factors affecting PNFs are well-known, scientific evidence on how cells (focus on the oral cavity) respond to them under physiological conditions is lacking. Self-assembled PNFs synthesized from fava bean whole protein isolate show a strong pH- and solvent-dependent morphology and elasticity modification measured by atomic force microscopy (AFM).
View Article and Find Full Text PDFBiophys J
December 2024
Institute for Medical Physics and Biophysics, University of Leipzig, Leipzig, Germany. Electronic address:
Cellular membranes exhibit a huge diversity of lipids and membrane proteins that differ in their properties and chemical structure. Cells organize these molecules into distinct membrane compartments characterized by specific lipid profiles and hydrophobic thicknesses of the respective domains. If a hydrophobic mismatch occurs between a membrane protein and the surrounding lipids, there can be functional consequences such as reduced protein activity.
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