In-vitro Selection of Highly Stabilized Protein Variants with Optimized Surface
Abstract
Thermostable proteins are of prime importance in protein science, but it has remained difficult to develop general strategies for stabilizing a protein. Site-directed mutagenesis based on comparisons with thermophilic homologs is rarely successful because the sequence differences are too numerous and dominated by neutral mutations. Here we used a method of directed evolution to increase the stability of a mesophilic protein, the cold shock...
Paper Details
Title
In-vitro Selection of Highly Stabilized Protein Variants with Optimized Surface
Published Date
Jun 1, 2001
Journal
Volume
309
Issue
3
Pages
717 - 726
Citation AnalysisPro
You’ll need to upgrade your plan to Pro
Looking to understand the true influence of a researcher’s work across journals & affiliations?
- Scinapse’s Top 10 Citation Journals & Affiliations graph reveals the quality and authenticity of citations received by a paper.
- Discover whether citations have been inflated due to self-citations, or if citations include institutional bias.
Notes
History