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• W1570451414 abstract "Publisher Summary In humans, the group I phospholipases A 2 (PLA 2 ) is present in the pancreas and the group II extracellular PLA 2 are found in platelets and arthritic synovial joints. The tertiary structure and disulfide bond pattern are similar among the two groups, with the following main differences: group II PLA 2 have an extension of approximately seven residues on the carboxy terminal part, which is also connected by a disulfide bond, group I PLA 2 have an insertion among the residues 54–56, and in group I the amino terminal helix is connected by a disulfide bond at residue 11. Recent nuclear magnetic resonance (NMR) determination of the solution structure of the pancreatic group I PLA 2 showed that, in contrast to the crystal structures, the beginning of the amino terminal helix is partly disordered. Moreover, the solution structure of the same PLA 2 complexed with the inhibitor and micelle displayed ordering of this region, which became more similar to the crystal structure. In this chapter, a NMR study has been performed on a group II PLA 2 from snake Agkistrodon piscivorus piscivorus , which has previously been extensively used in the biophysical studies on the membrane–protein interactions. In the present study, different techniques from the repertoire of the NMR methods have been used. Those techniques have provided independent data that are consistent and permitted reaching conclusion on the secondary structure of the protein. Improvement in production and refolding procedure for recombinant PLA 2 has allowed preparation of 13C and 15N labeled protein, allowing its assignment and measurement of several structural parameters that describe the conformation of the amino terminal helix. These parameters include NOE signal, main chain dihedral angles, coupling constants, amide hydrogen exchange rates and the deviation of the chemical shift, respectively. These data provide reliable conclusions about the secondary structure of the protein even before building the complete tertiary structure." @default.
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• W1570451414 date "1997-01-01" @default.
• W1570451414 modified "2023-09-27" @default.
• W1570451414 title "NMR confirms the presence of the aminoterminal helix of group II phospholipase A2 in solution" @default.
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• W1570451414 doi "https://doi.org/10.1016/s1080-8914(97)80062-2" @default.
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