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background-size: cover; background-repeat: no-repeat; | background-size: cover; background-repeat: no-repeat; | ||
background-position: 0 0, 0 -220px; | background-position: 0 0, 0 -220px; | ||
+ | } | ||
+ | } | ||
+ | |||
+ | @media(max-width:767px) { | ||
+ | .sidebar-nav { | ||
+ | text-align: center; | ||
+ | position: static; | ||
+ | top: 0; | ||
+ | } | ||
+ | } | ||
+ | |||
+ | @media(min-width:768px){ | ||
+ | .sidebar-nav{ | ||
+ | text-align: right; | ||
} | } | ||
} | } |
Revision as of 22:26, 16 October 2016
Human Practices
S-layer Engineering
The mesophilic organism Lysinibacillus sphaericus CCM 2177 produces the surface (S)-layer protein SbpA, which after secretion completely covers the cell surface with a crystalline array exhibiting square lattice symmetry. Because of its excellent in vitro recrystallization properties on solid supports, SbpA represents a suitable candidate for genetically engineering to create a versatile self-assembly system for the development of a molecular construction kit for nanobiotechnological applications. The first goal of this study was to investigate the surface location of 3 different C-terminal amino acid positions within the S-layer lattice formed by SbpA. Therefore, three derivatives of SbpA were constructed, in