Hydrophobic Core Malleability of a De Novo Designed Three-helix Bundle Protein
- 1 January 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 305 (2) , 361-373
- https://doi.org/10.1006/jmbi.2000.4184
Abstract
No abstract availableKeywords
This publication has 58 references indexed in Scilit:
- From coiled coils to small globular proteins: Design of a native‐like three‐helix bundleProtein Science, 1998
- De Novo Protein Design: Fully Automated Sequence SelectionScience, 1997
- Probing the role of packing specificity in protein designProceedings of the National Academy of Sciences, 1997
- Structure and Function of an Aromatic Ensemble That Restricts the Dynamics of the Hydrophobic Core of a Designed Helix-Loop-Helix DimerJournal of the American Chemical Society, 1997
- Protein Design: A Hierarchic ApproachScience, 1995
- Structural Determinants of Protein Dynamics: Analysis of 15N NMR Relaxation Measurements for Main-Chain and Side-Chain Nuclei of Hen Egg White LysozymeBiochemistry, 1995
- Thermodynamics of Denaturation of Barstar: Evidence for Cold Denaturation and Evaluation of the Interaction with Guanidine HydrochlorideBiochemistry, 1995
- Mutational analysis of the interaction between staphylococcal protein A and human IgG1Protein Engineering, Design and Selection, 1993
- Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperaturesBiochemistry, 1992
- Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studiesBiochemistry, 1989