Structure and function of integral membrane protein domains resolved by peptide-amphiphiles: Application to phospholamban

We have used synthetic lipidated peptides (“peptide‐amphiphiles”) to study the structure and function of isolated domains of integral transmembrane proteins. We used 9‐fluorenylmethyloxycarbonyl (Fmoc) solid‐phase peptide synthesis to prepare full‐length phospholamban (PLB1–52) and its cytoplasmic (...

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Veröffentlicht in:	Biopolymers 2003-07, Vol.69 (3), p.283-292
Hauptverfasser:	Lockwood, Nathan A., Tu, Raymond S., Zhang, Zhiwen, Tirrell, Matthew V., Thomas, David D., Karim, Christine B.
Format:	Artikel
Sprache:	eng
Schlagworte:	Buffers Ca-ATPase Calcium-Binding Proteins - chemical synthesis Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - metabolism Circular Dichroism co-reconstitution Hydrogen-Ion Concentration inhibitory effects Lipids - chemistry Liposomes membrane protein Membrane Proteins - chemical synthesis Membrane Proteins - chemistry Membrane Proteins - metabolism peptide modification peptide-amphiphile Peptides - chemical synthesis Peptides - chemistry phospholamban Protein Structure, Secondary Protein Structure, Tertiary secondary structure Structure-Activity Relationship
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