Structural Rearrangement from Oligomer to Fibril Detected with FRET in a Designed Amphiphilic Peptide
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DOI: 10.1002/cbic.201600436
Abstract: β‐Sheet conformation is promoted in peptides with amphiphilic design, and stable β‐turn formation is favored with the unnatural amino acid d‐Pro followed by a flexible residue such as Gly. A 19‐residue peptide (B3) was synthesized… read more here.
Keywords: oligomer fibril; fibril detected; rearrangement oligomer; detected fret ... See more keywords