Protonation of the Side Group in β- and γ-Aminated Proline Analogues: Effects on the Conformational Preferences-Reference-Cited by-同舟云学术

Protonation of the Side Group in β- and γ-Aminated Proline Analogues: Effects on the Conformational Preferences

Published:2009-03-18 Issue:8 Volume:74 Page:3101-3108
ISSN:0022-3263
Container-title:The Journal of Organic Chemistry
language:en
Short-container-title:J. Org. Chem.

Author:

Flores-Ortega Alejandra¹,Casanovas Jordi¹,Assfeld Xavier¹,Alemán Carlos¹

Affiliation:

1. Departament d’Enginyeria Química, E. T. S. d’Enginyeria Industrial de Barcelona, Universitat Politècnica de Catalunya, Avda. Diagonal no. 647, 08028 Barcelona, Spain, Departament de Química, Escola Politècnica Superior, Universitat de Lleida, c/Jaume II no. 69, 25001 Lleida, Spain, Chimie et Biochimie Théoriques, UMR CNRS UHP 7565, Institut Jean Barriol FR CNRS 2843, Faculté des Sciences et Techniques BP 70239, Nancy-Université, 54506 Vandoeuvre-lès-Nancy, France, and Center for Research in Nano...

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jo900169s

Reference48 articles.

1. Concepts and schemes for the re-engineering of physical protein modules: generating nanodevices via targeted replacements with constrained amino acids

2. Principles of nanostructure design with protein building blocks

3. Nanostructure Design Using Protein Building Blocks Enhanced by Conformationally Constrained Synthetic Residues

4. Use of Constrained Synthetic Amino Acids in β-Helix Proteins for Conformational Control

5. Structural Analysis of a β-Helical Protein Motif Stabilized by Targeted Replacements with Conformationally Constrained Amino Acids

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