Dispersion analysis of the orthorhombic peptide single crystal Z-(Aib)3-L-Ala-OtBu

Author:

Höfer Sonja,Berg Albrecht,Brückner Hans,Mayerhöfer Thomas G.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Elsevier BV

Subject

Spectroscopy,Instrumentation,Atomic and Molecular Physics, and Optics,Analytical Chemistry

Reference27 articles.

1. Introduction to protein crystallization;McPherson;Acta Crystallogr. Sect. F,2014

2. The crystal structure of Z-(Aib)10-OH at 0.65 Å resolution: three complete turns of 310-helix;Gessmann;J. Pept. Sci.,2016

3. The achiral tetrapeptide Z-Aib-Aib-Aib-Gly-OtBu;Gessmann;Acta Crystallographica Section C,2014

4. Nucleation, growth, and form in crystals of peptide helices;Vasudev;J. Phys. Chem. B,2008

5. R. Gessman, D. Axford, H. Brückner, A. Berg, and K. Petratos. A natural, single-residue substitution yields a less active peptabiotic: the structure of bergofungin A at atomic resolution. Acta Crystallogr. Sect. F, 73: 95–100, 2017.

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