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Activity and structural comparisons of solution associating and monomeric channel-forming peptides derived from the glycine receptor m2 segment.
Biophys J. 2004 Mar;86(3):1424-35. doi: 10.1016/S0006-3495(04)74212-5.
Biophys J. 2004.
PMID: 14990471
Free PMC article.
Distinct structural elements that direct solution aggregation and membrane assembly in the channel-forming peptide M2GlyR.
Broughman JR, Shank LP, Takeguchi W, Schultz BD, Iwamoto T, Mitchell KE, Tomich JM.
Broughman JR, et al.
Biochemistry. 2002 Jun 11;41(23):7350-8. doi: 10.1021/bi016053q.
Biochemistry. 2002.
PMID: 12044167
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Redesigning channel-forming peptides: amino acid substitutions that enhance rates of supramolecular self-assembly and raise ion transport activity.
Shank LP, Broughman JR, Takeguchi W, Cook G, Robbins AS, Hahn L, Radke G, Iwamoto T, Schultz BD, Tomich JM.
Shank LP, et al.
Biophys J. 2006 Mar 15;90(6):2138-50. doi: 10.1529/biophysj.105.070078. Epub 2005 Dec 30.
Biophys J. 2006.
PMID: 16387776
Free PMC article.
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