Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency-Reference-Cited by-同舟云学术

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Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency

Published:2010-06-11 Issue:26 Volume:107 Page:11686-11691
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Harrison R. S.,Shepherd N. E.,Hoang H. N.,Ruiz-Gomez G.,Hill T. A.,Driver R. W.,Desai V. S.,Young P. R.,Abbenante G.,Fairlie D. P.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference32 articles.

1. Structure, stability and folding of the α-helix

2. Exploring the sequence patterns in the -helices of proteins

3. Sequence and Structure Patterns in Proteins from an Analysis of the Shortest Helices: Implications for Helix Nucleation

4. The Mechanism of alpha-Helix Formation by Peptides

5. The Hydrogen Bond Mimic Approach: Solid-Phase Synthesis of a Peptide Stabilized as an α-Helix with a Hydrazone Link

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