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1PEF

PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE

Summary for 1PEF
Entry DOI10.2210/pdb1pef/pdb
DescriptorPEPTIDE F (EQLLKALEFLLKELLEKL) (2 entities in total)
Functional Keywordsalpha-helical bundle, synthetic protein
Total number of polymer chains1
Total formula weight2173.65
Authors
Garavito, R.M.,Taylor, K.,Yang, N.C. (deposition date: 1995-06-19, release date: 1996-12-07, Last modification date: 2024-02-14)
Primary citationTaylor, K.S.,Lou, M.Z.,Chin, T.M.,Yang, N.C.,Garavito, R.M.
A novel, multilayer structure of a helical peptide.
Protein Sci., 5:414-421, 1996
Cited by
PubMed Abstract: X-ray diffraction analysis at 1.5 A resolution has confirmed the helical conformation of a de novo designed 18-residue peptide. However, the crystal structure reveals the formation of continuous molecular layers of parallel-packed amphiphilic helices as a result of much more extensive helix-helix interactions than predicted. The crystal packing arrangement, by virtue of distinct antiparallel packing interactions, segregates the polar and apolar surfaces of the helices into discrete and well-defined interfacial regions. An extensive "ridges-into-grooves" interdigitation characterizes the hydrophobic interface, whereas an extensive network of salt bridges and hydrogen bonds dominates the corresponding hydrophilic interface.
PubMed: 8868477
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

226707

건을2024-10-30부터공개중

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