1PEF

PEPTIDE F (EQLLKALEFLLKELLEKL), AMPHIPHILIC OCTADECAPEPTIDE

Summary for 1PEF

• Entry DOI: 10.2210/pdb1pef/pdb
• Descriptor: PEPTIDE F (EQLLKALEFLLKELLEKL) (2 entities in total)
• Functional Keywords: alpha-helical bundle, synthetic protein
• Total number of polymer chains: 1
• Total formula weight: 2173.65

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 citation

Taylor, 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

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)