Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide‐rich de novo designed peptides
Sign Up to like & getrecommendations! Published in 2018 at "Protein Science"
DOI: 10.1002/pro.3453
Abstract: Disulfide‐rich peptides represent an important protein family with broad pharmacological potential. Recent advances in computational methods have made it possible to design new peptides which adopt a stable conformation de novo. Here, we describe a… read more here.
Keywords: novo designed; disulfide rich; solution; rich novo ... See more keywords
Cu(I) Binding to Designed Proteins Reveals a Putative Copper Binding Site of the Human Line1 Retrotransposon Protein ORF1p.
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DOI: 10.1021/acs.inorgchem.2c00057
Abstract: Long interspersed nuclear elements-1 (L1) are autonomous retrotransposons that encode two proteins in different open reading frames (ORF1 and ORF2). The ORF1p, which may be an RNA binding and chaperone protein, contains a three-stranded coiled… read more here.
Keywords: designed peptides; copper binding; domain; copper ... See more keywords
Designed peptides that assemble into cross-α amyloid-like structures
Sign Up to like & getrecommendations! Published in 2018 at "Nature Chemical Biology"
DOI: 10.1038/s41589-018-0105-5
Abstract: Amyloids adopt ‘cross-β’ structures composed of long, twisted fibrils with β-strands running perpendicular to the fibril axis. Recently, a toxic peptide was proposed to form amyloid-like cross-α structures in solution, with a planar bilayer-like assembly… read more here.
Keywords: amyloid; amyloid like; like structures; peptides assemble ... See more keywords