1pef

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pef OCA], [https://pdbe.org/1pef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pef RCSB], [https://www.ebi.ac.uk/pdbsum/1pef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pef ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

A novel, multilayer structure of a helical peptide.,Taylor KS, Lou MZ, Chin TM, Yang NC, Garavito RM Protein Sci. 1996 Mar;5(3):414-21. PMID:8868477<ref>PMID:8868477</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1pef" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Garavito, R M]]

[[Category: Taylor, K]]

[[Category: Yang, N C]]

[[Category: Synthetic protein]]