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・ Beta-Carotene
・ Beta-carotene 15,15'-dioxygenase
・ Beta-carotene 15,15'-monooxygenase
・ Beta-carotene 3-hydroxylase
・ Beta-carotene isomerase
・ Beta-catenin
・ Beta-chamigrene synthase
・ Beta-copaene synthase
・ Beta-cubebene synthase
・ Beta-cyclopiazonate dehydrogenase
・ Beta-D
・ Beta-D-fucosidase
・ Beta-D-galactosyl-(1-4)-L-rhamnose phosphorylase
・ Beta-D-glucopyranosyl abscisate beta-glucosidase
・ Beta-decay stable isobars
Beta-defensin 2
・ Beta-diketone hydrolase
・ Beta-dual space
・ Beta-Eleostearic acid
・ Beta-Endorphin
・ Beta-Ergocryptine
・ Beta-eudesmol synthase
・ Beta-farnesene synthase
・ Beta-galactofuranosidase
・ Beta-galactosidase
・ Beta-galactoside alpha-2,3-sialyltransferase
・ Beta-galactoside alpha-2,6-sialyltransferase
・ Beta-galactoside permease
・ Beta-galactoside transacetylase
・ Beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase


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Beta-defensin 2 : ウィキペディア英語版
Beta-defensin 2

Beta-defensin 2 (BD-2) also known as skin-antimicrobial peptide 1 (SAP1) is a peptide that in humans is encoded by the ''DEFB4'' (defensin, beta 4) gene.
Human beta-defensin-2 (hBD-2) is a cysteine-rich cationic low molecular weight antimicrobial peptide recently discovered in lesional skin.
== Structure ==

hBD-2 is a protein whose primary structure is made by 64 aminoacids. At concentrations ≤2.4 mM, hBD-2 is monomeric. The structure is amphiphilic with a nonuniform surface distribution of positive charge and contains several key structural elements, including a triple-stranded, antiparallel beta sheet with strands 2 and 3 in a beta hairpin conformation.
The determination of other structural elements depends on the technique used. When X-ray crystallography is used an alpha helix can be observed at the C-terminal end of the protein (PDB code: ). When using NMR this alpha-helix does not appear (PDB code: ).

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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