White SH; Wimley WC; (1999) Membrane Protein Folding
and Stability:Physical Principles. Annual Reviews of Biophysics
and Biomolecular Structure 28:319-65. Medline
Citation
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White SH; Wimley WC; (1999) Membrane Protein Folding
and Stability:Physical Principles. Annual Reviews of Biophysics
and Biomolecular Structure 28:319-65. Medline
Citation |
Peptide insertion and folding in membranes is driven mainly hydrophobic interactions. However these interactions also drive precipitation and insolubility of peptides in water (states b, d and g). A good experimental design includes tests for the aggregation state and structure of a peptide in solution as well as the peptide's structure, orientation and aggregation state in membranes. A membrane-bound peptide can be interfacial (states c and e) or transmembrane (states f and h). In either case the peptide can be monomeric or multimeric. In our research we are designing peptides that bind and assemble in membranes into specific types of structures. |
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