Beyond Consensus: Statistical Free Energies Reveal Hidden Interactions in the Design of a TPR Motif
- 22 October 2004
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 343 (3) , 731-745
- https://doi.org/10.1016/j.jmb.2004.08.026
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Structure-based substitutions for increased solubility of a designed proteinProtein Engineering, Design and Selection, 2003
- Designed to be stable: Crystal structure of a consensus ankyrin repeat proteinProceedings of the National Academy of Sciences, 2003
- Consensus-derived structural determinants of the ankyrin repeat motifProceedings of the National Academy of Sciences, 2002
- The consensus concept for thermostability engineering of proteins: further proof of conceptProtein Engineering, Design and Selection, 2002
- Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides 1 1Edited by I. A. WilsonJournal of Molecular Biology, 2000
- From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytaseProtein Engineering, Design and Selection, 2000
- Intrabody construction and expression. II. A synthetic catalytic Fv fragmentJournal of Molecular Biology, 1999
- Intrabody construction and expression. I. The critical role of VL domain stabilityJournal of Molecular Biology, 1999
- Sequence Statistics Reliably Predict Stabilizing Mutations in a Protein DomainJournal of Molecular Biology, 1994
- Use of a zinc-finger consensus sequence framework and specificity rules to design specific DNA binding proteins.Proceedings of the National Academy of Sciences, 1993