X-ray crystal structure of conformationally constrained pentapeptide Boc-Pro-dehydro-Phe-Ala-dehydro-Phe-Ala-OMe
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چکیده
منابع مشابه
Infinite pleated -sheet formed by the -hairpin Boc- -Phe- -Phe-D-Pro-Gly- -Phe- -Phe-OMe
A -hairpin conformation and extended -pleated sheet assembly have been characterized by single crystal x-ray diffraction for the synthetic peptide t-butoxycarbonyl— -Phe-Phe-D-Pro-GlyPhe-Phe-methyl ester [ -Phe: (S)3 homophenylalanine]. The centrally located D-Pro-Gly segment nucleates a chain reversal in a type II -turn conformation. Two intramolecular cross-strand hydrogen bonds stabilize the...
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THE TITLE COMPOUND (SYSTEMATIC NAME tert-butyl 3-{[1-(methoxy-carbon-yl)eth-yl]amino-carbon-yl}-3-methyl-carbazate), C(11)H(21)N(3)O(5), is a precursor for the study of a new class of foldamer based on aza/α-dipeptide oligomerization [Abbas et al. (2009 ▶). Tetra-hedron Lett.50, 4158-4160]. The asymmetric unit consists of one mol-ecule in an extended conformation which is stabilized by inter-mo...
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In the title compound, phenyl (S)-2-[(S)-(1-{2-[(S)-(1-{[(tert-but-oxy)carbon-yl]amino}-bicyclo-[2.2.2]octan-2-yl)formamido]-propanamido}-bicyclo-[2.2.2]octan-2-yl)formamido]-3-phenyl-propano-ate chloro-form monosolvate, C42H56N4O7·CHCl3, the α,β-hybrid peptide contains two non-proteinogenic amino acid residues of (S)-1-amino-bicyclo-[2.2.2]octane-2-carb-oxy-lic acid [(S)-ABOC], two amino acid ...
متن کاملAromatic-aromatic interactions in crystal structures of helical peptide scaffolds containing projecting phenylalanine residues.
Aromatic-aromatic interactions between phenylalanine side chains in peptides have been probed by the structure determination in crystals of three peptides: Boc-Val-Ala-Phe-Aib-Val-Ala-Phe-Aib-OMe, I; Boc-Val-Ala-Phe-Aib-Val-Ala-Phe-Aib-Val-Ala-Phe-Aib-OMe, II; Boc-Aib-Ala-Phe-Aib-Phe-Ala-Val-Aib-OMe, III. X-ray diffraction studies reveal that all three peptides adopt helical conformations in th...
متن کاملInhibition of proteinase K by methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone. An x-ray study at 2.2-A resolution.
The crystal structure of the transition state analog complex formed covalently between proteinase K and methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone was determined by x-ray diffraction methods at a resolution of 2.2 A and refined by constrained least squares to an R factor of 19.8% for the 11864 structure amplitudes greater than 1 sigma F. The chloromethyl ketone group is covalently link...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 1993
ISSN: 0108-7673
DOI: 10.1107/s0108767378095902