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・ Beta-Neoendorphin
・ Beta-nitroacrylate reductase
・ Beta-Nitropropionic acid
・ Beta-Nitrostyrene
・ Beta-peptide
・ Beta-peptidyl aminopeptidase
・ Beta-phellandrene synthase (neryl-diphosphate-cyclizing)
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・ Beta-Pinene
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Beta-sandwich
・ Beta-santalene synthase
・ Beta-seco-amyrin synthase
・ Beta-secretase
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・ Beta-secretase 2
・ Beta-selinene cyclase
・ Beta-sesquiphellandrene synthase
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・ Beta-Tocopherol
・ Beta-Tocotrienol


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Beta-sandwich : ウィキペディア英語版
Beta-sandwich

β-sandwich domains are characterized by two opposing antiparallel β-sheets. The number of strands found in the sandwich motif may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds. The immunoglobulin-type fold found in antibodies (Ig-fold) consists of a sandwich arrangement of 7 and 9 antiparallel β-strands arranged in two β-sheets with a Greek-key topology. The Greek-key topology is also found in Human Transthyretin. The jelly-roll topology is found in
carbohydrate binding proteins such as concanavalin A and various lectins, in the collagen binding domain of ''Staphylococcus aureus'' Adhesin and in modules that bind fibronectin as found in Tenascin (Third Fibronectin Type III Repeat).
The L-type lectin domain is a variation of the jelly roll fold. The C2 domain in its typical version (PKC-C2) is a β-sandwich composed of 8 β-strands.
==References==


抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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