Journal of the American Chemical Society
Article
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(35) This virtual dihedral (ϖ) was previously used to describe the
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see: (a) Greenfield, S. J.; Agarkov, A.; Gilbertson, S. R. Org. Lett. 2003,
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Biopolymers 2006, 84, 48−73. (d) Revell, J. D.; Wennemers, H. Adv.
Synth. Catal. 2008, 350, 1046−1052. (e) Akagawa, K.; Akabane, H.;
Sakamoto, S.; Kudo, K. Org. Lett. 2008, 10, 2035−2037. (f) Wiesner,
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(41) The batch of peptide 16 that gave rise to polymorphs 16a,b and
16c was catalytically competent in the atroposelective bromination of
1 described in eq 1. Additionally, the NMR spectrum of 16 is
consistent with protonated catalyst (see the Supporting Information).
As such, it is unlikely that our stock of 16c is protonated. The source
of the HCl equivalents remains unclear, but we speculate that the
16a,b crystal may have nucleated on a grain of adventitious, wet NaCl.
(42) For a computational study of cyclobutane puckering, see:
Glendening, E. D.; Halpern, A. M. J. Phys. Chem. A 2005, 109, 635−
642.
(43) Zhou, A. Q.; O’Hern, C. S.; Regan, L. Protein Sci. 2011, 20,
Marcelli, T.; Himo, F. ACS Catal. 2016, 6, 1165−1171. (l) Grunen-
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̈
(44) Grunenfelder, C. E.; Kisunzu, J. K.; Trapp, N.; Kastl, R.;
felder, C. E.; Kisunzu, J. K.; Wennemers, H. Angew. Chem., Int. Ed.
2016, 55, 8571−8574. (m) Ueda, A.; Umeno, T.; Doi, M.; Akagawa,
K.; Kudo, K.; Tanaka, M. J. Org. Chem. 2016, 81, 6343−6356.
(28) (a) Diener, M. E.; Metrano, A. J.; Kusano, S.; Miller, S. J. J. Am.
Chem. Soc. 2015, 137, 12369−12377. (b) Metrano, A. J.; Abascal, N.
C.; Mercado, B. Q.; Paulson, E. K.; Miller, S. J. Chem. Commun. 2016,
52, 4816−4819.
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Wennemers, H. Biopolymers (Pept. Sci.) 2016, ASAP, DOI: 10.1002/
(45) Steiner, T. Acta Crystallogr., Sect. B: Struct. Sci. 2000, B56, 673−
676.
(46) (a) Choi, S. H.; Guzei, I. A.; Spencer, L. C.; Gellman, S. H. J.
Am. Chem. Soc. 2010, 132, 13879−13885. (b) Choi, S. H.; Guzei, I. A.;
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(29) For peptide 34: (a) Blank, J. T.; Miller, S. J. Biopolymers 2006,
84, 38−47. For peptide 35, see ref 9a. For peptide 36: (b) Jakobsche,
C. E.; Peris, G.; Miller, S. J. Angew. Chem., Int. Ed. 2008, 47, 6707−
6711. For peptide 37: (c) Blank, J. T.; Guerin, D. J.; Miller, S. J. Org.
Lett. 2000, 2, 1247−1249.
(30) A search of the Cambridge Structural Database (CSD) on 17
October 2016 returned 424 Pro-Xaa-containing peptides, about half of
which were cyclic. Of the 191 noncyclic entries: (1) 54 contained α,α-
disubstituted residues as Xaa; (2) 12 contained Acpc as Xaa; and (3)
19 were tetramers.
(47) Thompson, H. P. G.; Day, G. M. Chem. Sci. 2014, 5, 3173−
3182.
(48) For a discussion of amide pyramidalization in proteins, see:
(a) MacArthur, M. W.; Thornton, J. M. J. Mol. Biol. 1996, 264, 1180−
1195. For related examples, see: (b) Cruz-Cabeza, A. J.; Day, G. M.;
Motherwell, W. D. S.; Jones, W. Cryst. Growth Des. 2006, 6, 1858−
1866. (c) Aleman
Casanovas, J. J. Phys. Chem. B 2005, 109, 11836−11841.
́ ́ ́
, C.; Jimenez, A. I.; Cativiela, C.; Perez, J. J.;
X
J. Am. Chem. Soc. XXXX, XXX, XXX−XXX