Pub. Date : 2017 Oct 10
PMID : 28876052
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | 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 | hematopoietically expressed homeobox | Homo sapiens |
| 2 | 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 | hematopoietically expressed homeobox | Homo sapiens |
| 3 | 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 | hematopoietically expressed homeobox | Homo sapiens |
| 4 | 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 | hematopoietically expressed homeobox | Homo sapiens |
| 5 | 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 | hematopoietically expressed homeobox | Homo sapiens |