Intricacies of β Sheet Protein Design

Julia M. Shifman

doi:10.1016/j.str.2008.11.001

Intricacies of β Sheet Protein Design

Julia M. Shifman^*

^*Corresponding author for this work

Department of Biological Chemistry

Research output: Contribution to journal › Short survey › peer-review

3 Scopus citations

Abstract

Design of soluble and monomeric β sheet proteins remains a challenge due to the high propensity of such proteins to misfold and aggregate. This challenge was overcome by Hu et al. (2008), who report a full-sequence redesign of the largest up-to-date β sheet protein with a verified three-dimensional structure.

Original language	English
Pages (from-to)	1751-1752
Number of pages	2
Journal	Structure
Volume	16
Issue number	12
DOIs	https://doi.org/10.1016/j.str.2008.11.001
State	Published - 12 Dec 2008

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AB - Design of soluble and monomeric β sheet proteins remains a challenge due to the high propensity of such proteins to misfold and aggregate. This challenge was overcome by Hu et al. (2008), who report a full-sequence redesign of the largest up-to-date β sheet protein with a verified three-dimensional structure.

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Intricacies of β Sheet Protein Design

Abstract

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