Molecular biology of membranes: structure and function

1994 ◽  
Vol 4 (1) ◽  
pp. 32-33
Author(s):  
Richard J. Cherry
2019 ◽  
Vol 1 (1) ◽  
pp. 1-3
Author(s):  
Venki Ramakrishnan ◽  
Mejd Alsari

Venkatraman ‘Venki’ Ramakrishnan is the President of The Royal Society and Group Leader at the MRC Laboratory of Molecular Biology. In 2009 he shared the Nobel Prize in Chemistry ‘for studies of the structure and function of the ribosome’. In this interview he explains why governments should invest more in basic scientific research rather than simply on applied science and engineering. He also discusses interdisciplinarity, collaborations, and public engagement.


1995 ◽  
Vol 269 (5) ◽  
pp. G613-G627 ◽  
Author(s):  
B. J. Van Klinken ◽  
J. Dekker ◽  
H. A. Buller ◽  
A. W. Einerhand

The cloning of mucin cDNAs brought about by the application of molecular biology and molecular analyses constitutes a major step in understanding mucin structure and function. Here two classes of mucins are described: epithelium-associated and endothelium/leukocyte-associated mucins, which have thus far been described separately in the literature. The epithelial mucins are generally believed to play a role in cytoprotection. The endothelial and leukocyte class of mucins are adhesion molecules involved in lymphocyte homing and lymphocyte activation or are part of the adhesion cascade that plays a role in the initiation of inflammation. Mucins in general contain many threonine and serine residues, which are extensively O-glycosylated. Due to this profound glycosylation, mucins have a filamentous conformation. By virtue of their extended filamentous, and often negatively charged, structure, mucins can act as a barrier protecting the cell. However, when an opposing cell has specific receptors for mucins, adhesion can override the barrier function. Therefore, mucins may be powerful two-edged swords: they are both protective and adhesive.


2019 ◽  
pp. 217-240
Author(s):  
Gordon L. Fain

“Extra sensory receptors” is the tenth chapter of the book Sensory Transduction and reviews mechanisms of sensory transduction in three additional sensory modalities: thermoreception, electroreception, and magnetoreception. It describes the physiology and molecular biology of warm and cold receptors in the mammalian skin, including the channels thought to be responsible and mechanisms of channel gating. There follows an extensive description of thermoreceptors in the pit organs of snakes which permit these animals literally to see in the dark. The section on electroreception reviews in detail the mechanism responsible for the astonishing sensitivity of the ampullary receptors of skates, as well as the structure and function of tuberous receptors, electrocytes, and electrolocation. The final section on magnetoreception describes magnetotactic bacteria as well as the evidence for magnetoreception in migrating birds, together with theories—as yet unproved—for the mechanism of animal sensitivity to magnetic fields.


1991 ◽  
Vol 11 (6) ◽  
pp. 445-475 ◽  
Author(s):  
Peter B. Garland

The concept of chemiosmotic systems arises from the pioneering work of Peter Mitchell on two fronts. One is concerned with the mechanisms by which molecules are transported across membranes which are generally barriers to such transport. These mechanisms are inevitably molecular, and are now yielding their secrets to a combination of structural protein chemistry and molecular biology. The other front is more physiological, and explores the functional relationships between metabolism and transport. Nevertheless, the two fronts form a continuum of mutally related structure and function. Chemiosmotic systems provide a hierarchy of complexity, starting from say a uniporter reconstituted in a chemically defined bilayer, and proceeding to greater complexity in mitochondria, chloroplasts, eukaryotic and prokaryotic cell membranes, and multicellular systems. Their relationship to medicine is profound, because they provide many opportunities for therapeutic intervention. In this paper I present an overview of chemiosmotic systems at different levels of complexity, both molecular and biological, of their involvements in pathology, and of possible pharmacological treatment or prevention of disease.


2014 ◽  
Vol 70 (a1) ◽  
pp. C935-C935
Author(s):  
Thomas Steitz

Max Perutz's Dunham Lectures at Harvard in 1963, in which he showed the first atomic structure of a protein (myoglobin) that anyone in the room had ever seen, led to my working on the structure of carboxypeptidase A (CPA) (in the Lipscomb lab) before going to the MRC LMB in Cambridge. "Rapid" data collection on CPA in the mid-1960s was 5,000 reflections in a week, and now obtaining 2.7 Å resolution data on crystals with two 70S ribosomes in the asymmetric unit takes 5 minutes. Importantly, the LMB promoted creative and novel science because of its cooperative, interactive atmosphere where everyone interacted in the hall or over coffee, lunch or tea. This influenced how I have carried out science over the subsequent years. In the canteen, Crick, Brenner, Perutz, etc., would be interacting and talking with postdocs and students about asking important questions and solving scientific problems. It was a great place to learn, develop and use the most advanced methods in protein crystallography and apply them to explore the most interesting and significant questions in molecular biology. The importance of integrating structure and function in our research goals was made clear. My interactions in the Cambridge LMB led me to pursue the structural basis for understanding Crick's Central Dogma of Molecular Biology – DNA makes DNA makes RNA makes proteins. This resulted in our ultimately determining the structures of the ribosome and its various complexes.


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