Sandbox 174: Difference between revisions
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The overall size of the molecule is 40 x 30 x 20 Å, with two outer loops folded toward one another. α-BGT is "flat" enough to contain no hydrophobic core, but does contain a few uncharged sidechain groupings<ref name="main">Love, A.R. and Stroud, R.M. (1986) The Crystal Structure of α-Bungarotoxin at 2.5 Å resolution: Relation to Solution Structure and Binding to Acetylcholine Receptor. ''Protein Eng'' '''1''', 37-46.</ref>. | The overall size of the molecule is 40 x 30 x 20 Å, with two outer loops folded toward one another. α-BGT is "flat" enough to contain no hydrophobic core, but does contain a few uncharged sidechain groupings<ref name="main">Love, A.R. and Stroud, R.M. (1986) The Crystal Structure of α-Bungarotoxin at 2.5 Å resolution: Relation to Solution Structure and Binding to Acetylcholine Receptor. ''Protein Eng'' '''1''', 37-46.</ref>. | ||
The protein is a dimer, and consists of two seperate subunits: | The protein is a dimer, and consists of two seperate subunits: | ||
<scene name='Sandbox_174/Domain_b/ | <scene name='Sandbox_174/Domain_b/4'>Domain A</scene> | ||
<scene name='Sandbox_174/Domain_a/ | <scene name='Sandbox_174/Domain_a/4'>Domain B</scene> | ||