ORCID Profile
0000-0003-2460-1145
Current Organisation
Universidade Estadual Paulista Júlio de Mesquita Filho
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Publisher: Universitas Sam Ratulangi
Date: 21-01-2022
Abstract: Tumumpa Coastal Fishing Port is located at 1°31'21"-1°31'35" N, 124°50'28"-124°51'24" E Tides are one of the phenomena that can be utilized as a reference in determining natural resource management policies and as a supplement to data used to forecast future marine conditions. Using the Least Squares Method and the Admiralty Method with 15 days of observation data, the analysis was undertaken with the goal of finding the phase and litude of tidal components, type of tides, and the elevation of sea level at Tumumpa Coastal Fishing Port. The tidal type at the port is mixed semidiurnal tides, the formzahl value for the least square method is 0.48, while for the Admiralty method is 0.39Keywords: Tides Formzahl RMSE PPP Tumumpa.AbstrakPasang surut air laut merupakan salah satu fenomena yang bisa dijadikan referensi dalam penentuan kebijakan untuk pengelolaan sumber daya alam dan sebagai data pelengkap untuk menggambarkan kondisi laut pada masa mendatang. Tujuan dari penelitian ini adalah untuk menganalisis komponen-komponen pasang surut dan tipe pasang surut yang diukur di Pelabuhan Perikanan Pantai (PPP) Tumumpa. Analisis dengan menggunakan metode kuadrat terkecil dan metode Admiralty berdasarkan data 15 hari pengamatan. Hasil penelitian menunjukkan bahwa tipe pasang surut di PPP Tumumpa bertipe c uran condong harian ganda. Didapatkan dominasi komponen harmonik pasang surut pada PPP Tumumpa, bertipe c uran condong harian ganda. Komponen harmonik pasang surut dominan di PPP Tumumpa, yaitu komponen semidiurnal untuk metode kuadrat terkecil M2 = 0.21 dan S2= 1.47 sedangkan untuk metode Admiralty M2 = 52.08 dan S2= 34.59.Kata kunci: Pasang surut Nilai Formzahl RMSE PPP Tumump
Publisher: Elsevier BV
Date: 02-2005
DOI: 10.1016/J.BIOCHI.2004.11.005
Abstract: The crystal structure of dimeric Lys49-phospholipase A2 myotoxin-II from Bothrops moojeni (MjTX-II) co-crystallized with stearic acid (C(18)H(36)O(2)) has been determined at a resolution of 1.8 A. The electron density maps permitted the unambiguous inclusion of six stearic acid molecules in the refinement. Two stearic acid molecules could be located in the substrate-binding cleft of each monomer in positions, which favor the interaction of their carboxyl groups with active site residues. The way of binding of stearic acids to this Lys49-PLA(2)s is analogous to phospholipids and transition state analogues to catalytically active PLA(2)s. Two additional stearic acid molecules were located at the dimer interface region, defining a hitherto unidentified acyl-binding site on the protein surface. The strictly conserved Lys122 for Lys49-PLA(2)s may play a fundamental role for stabilization of legend-protein complex. The comparison of MjTX-II/satiric acid complex with other Lys-PLA(2)s structures whose putative fatty acids were located at their active site is also analysed. Molecular details of the stearic acid rotein interactions provide insights to binding in group I/II PLA(2)s, and to the possible interactions of Lys49-PLA(2)s with target membranes.
Publisher: Springer Science and Business Media LLC
Date: 16-05-2016
Publisher: Wiley
Date: 17-05-2011
DOI: 10.1111/J.1742-4658.2011.08115.X
Abstract: Snake venoms are cocktails of enzymes and non-enzymatic proteins used for both the immobilization and digestion of prey. The most common snake venom enzymes include acetylcholinesterases, l-amino acid oxidases, serine proteinases, metalloproteinases and phospholipases A(2) . Higher catalytic efficiency, thermal stability and resistance to proteolysis make these enzymes attractive models for biochemists, enzymologists and structural biologists. Here, we review the structures of these enzymes and describe their structure-based mechanisms of catalysis and inhibition. Some of the enzymes exist as protein complexes in the venom. Thus we also discuss the functional role of non-enzymatic subunits and the pharmacological effects of such protein complexes. The structures of inhibitor-enzyme complexes provide ideal platforms for the design of potent inhibitors which are useful in the development of prototypes and lead compounds with potential therapeutic applications.
Publisher: Elsevier BV
Date: 10-2004
Location: Brazil
Location: Germany
No related grants have been discovered for Raghuvir Arni.