PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28876052-2 2017 A recently discovered antiparallel coiled-coil hexamer (ACC-Hex, peptide 1) exhibits a unique interaction in which Phe and Ile residues from adjacent alpha-helices interact to form a Phe-Ile zipper within the hydrophobic core. Phenylalanine 115-118 hematopoietically expressed homeobox Homo sapiens 60-63 31517530-4 2019 Results & conclusions: The binding free energy (DeltaGbind) and the change in the free energy surface (FES) computed from the funnel metadynamics (FMD) simulation, both support the idea that inhibitors (-)-phe and (-)-hex have better binding activities toward enzyme AChE, and that (-)-phe is stronger in binding than the present AD drug (-)-phy. Phenylalanine 206-209 hematopoietically expressed homeobox Homo sapiens 218-221 31517530-4 2019 Results & conclusions: The binding free energy (DeltaGbind) and the change in the free energy surface (FES) computed from the funnel metadynamics (FMD) simulation, both support the idea that inhibitors (-)-phe and (-)-hex have better binding activities toward enzyme AChE, and that (-)-phe is stronger in binding than the present AD drug (-)-phy. Phenylalanine 286-289 hematopoietically expressed homeobox Homo sapiens 218-221 28876052-2 2017 A recently discovered antiparallel coiled-coil hexamer (ACC-Hex, peptide 1) exhibits a unique interaction in which Phe and Ile residues from adjacent alpha-helices interact to form a Phe-Ile zipper within the hydrophobic core. Phenylalanine 183-186 hematopoietically expressed homeobox Homo sapiens 60-63 28876052-3 2017 Analysis of the X-ray crystallographic structure of ACC-Hex suggests that the stability of the six-helix bundle relies on specific interactions between the Phe and Ile residues. Phenylalanine 156-159 hematopoietically expressed homeobox Homo sapiens 56-59 28876052-6 2017 Using size exclusion chromatography and small-angle X-ray scattering, we found that the proper assembly of ACC-Hex from monomers is sensitive to subtle changes in side chain steric bulk and hydrophobicity introduced by mutations at the Phe and Ile residue positions. Phenylalanine 236-239 hematopoietically expressed homeobox Homo sapiens 111-114 28876052-9 2017 Finally, we expanded on the generality of the Phe-Ile zipper, creating a unique sequence that forms an antiparallel hexamer that is topologically similar to ACC-Hex but atomistically unique. Phenylalanine 46-49 hematopoietically expressed homeobox Homo sapiens 161-164