The membrane interface as a structured compartment and a substrate for enzyme action
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The membrane interface as a structured compartment and a substrate for enzyme action. / Mouritsen, Ole G.; Bagatolli, Luis A.; Simonsen, Adam C.
Structure and Dynamics of Membranous Interfaces. Wiley-Interscience, 2014. p. 3-17.Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
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TY - CHAP
T1 - The membrane interface as a structured compartment and a substrate for enzyme action
AU - Mouritsen, Ole G.
AU - Bagatolli, Luis A.
AU - Simonsen, Adam C.
PY - 2014/1/1
Y1 - 2014/1/1
N2 - This chapter reviews some of the results that have been obtained in our laboratories with regard to characterization of lateral order in model bilayer membranes as well as biological membranes, with particular focus on membrane domains in the submicron regime. The results are based mainly on fluorescence microscopy and two‐photon laser scanning microscopy as well as atomic force microscopy (AFM). The chapter then shows by a specific example how a small enzyme, secretory phospholipase A2 (s‐PLA2) becomes activated at membrane interfaces in a way that is controlled by the lateral structure of the lipid‐bilayer substrate. This serves as a clear‐cut example of how certain collective properties of a lipid assembly are marshalling the function of a protein, hence highlighting the importance of lipids for membrane function. It furthermore shows how novel instrumentation and imaging techniques open up a new window to allow for quantitative description of biochemical processes.
AB - This chapter reviews some of the results that have been obtained in our laboratories with regard to characterization of lateral order in model bilayer membranes as well as biological membranes, with particular focus on membrane domains in the submicron regime. The results are based mainly on fluorescence microscopy and two‐photon laser scanning microscopy as well as atomic force microscopy (AFM). The chapter then shows by a specific example how a small enzyme, secretory phospholipase A2 (s‐PLA2) becomes activated at membrane interfaces in a way that is controlled by the lateral structure of the lipid‐bilayer substrate. This serves as a clear‐cut example of how certain collective properties of a lipid assembly are marshalling the function of a protein, hence highlighting the importance of lipids for membrane function. It furthermore shows how novel instrumentation and imaging techniques open up a new window to allow for quantitative description of biochemical processes.
UR - http://www.scopus.com/inward/record.url?scp=77956393429&partnerID=8YFLogxK
U2 - 10.1002/9780470388495.ch1
DO - 10.1002/9780470388495.ch1
M3 - Book chapter
AN - SCOPUS:77956393429
SN - 9780470388518
SP - 3
EP - 17
BT - Structure and Dynamics of Membranous Interfaces
PB - Wiley-Interscience
ER -
ID: 259011651