Tolerance of the archaeal Sac7d scaffold protein to alternative library designs: characterization of anti-immunoglobulin G Affitins-Reference-Cited by-同舟云学术

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Tolerance of the archaeal Sac7d scaffold protein to alternative library designs: characterization of anti-immunoglobulin G Affitins

Published:2013-01-11 Issue:4 Volume:26 Page:267-275
ISSN:1741-0126
Container-title:Protein Engineering Design and Selection
language:en
Short-container-title:Protein Engineering Design and Selection

Author:

Behar G.,Bellinzoni M.,Maillasson M.,Paillard-Laurance L.,Alzari P. M.,He X.,Mouratou B.,Pecorari F.

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/26/4/267/4355747/gzs106.pdf

Reference46 articles.

1. OB-fold domains: a snapshot of the evolution of sequence, structure and function

2. Role of a Surface Tryptophan in Defining the Structure, Stability, and DNA Binding of the Hyperthermophile Protein Sac7d,

3. Engineering novel binding proteins from nonimmunoglobulin domains

4. Type II Secretion System Secretin PulD Localizes in Clusters in the Escherichia coli Outer Membrane

5. Probing the DNA kink structure induced by the hyperthermophilic chromosomal protein Sac7d

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