Toward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme.
Biochemistry (1991)
;Cumulative Site-Directed Charge-Change Replacements in Bacteriophage T4 Lysozyme Suggest that Long-Range Electrostatic Interactions Contribute Little to Protein Stability
;
J.Mol.Biol. (1991)
;Analysis of the Interaction between Charged Side Chains and the Alpha-Helix Dipole Using Designed Thermostable Mutants of Phage T4 Lysozyme
;
Biochemistry (1991)
Structural and Thermodynamic Analysis of the Packing of Two Alpha-Helices in Bacteriophage T4 Lysozyme
J.Mol.Biol. (1991)
Contributions of Engineered Surface Salt Bridges to the Stability of T4 Lysozyme Determined by Directed Mutagenesis
Biochemistry (1991)
;Structure of a Thermostable Disulfide-Bridge Mutant of Phage T4 Lysozyme Shows that an Engineered Crosslink in a Flexible Region Does not Increase the Rigidity of the Folded Protein
;
Biochemistry (1990)
Structural Studies of Mutants of T4 Lysozyme that Alter Hydrophobic Stabilization
J.Biol.Chem. (1989)
High-Resolution Structure of the Temperature-Sensitive Mutant of Phage Lysozyme, Arg 96 (Right Arrow) His
Biochemistry (1989)
Contributions of Left-Handed Helical Residues to the Structure and Stability of Bacteriophage T4 Lysozyme
J.Mol.Biol. (1989)
Hydrophobic Stabilization in T4 Lysozyme Determined Directly by Multiple Substitutions of Ile 3
Nature (1988)
Enhanced Protein Thermostability from Designed Mutations that Interact with Alpha-Helix Dipoles
Nature (1988)
Replacements of Pro86 in Phage T4 Lysozyme Extend an Alpha-Helix But Do not Alter Protein Stability
Science (1988)
Enhanced Protein Thermostability from Site-Directed Mutations that Decrease the Entropy of Unfolding
Proc.Natl.Acad.Sci.USA (1987)
Structural Analysis of the Temperature-Sensitive Mutant of Bacteriophage T4 Lysozyme, Glycine 156 (Right Arrow) Aspartic Acid
J.Biol.Chem. (1987)
Contributions of Hydrogen Bonds of Thr 157 to the Thermodynamic Stability of Phage T4 Lysozyme
Nature (1987)
;Structural Studies of Mutants of the Lysozyme of Bacteriophage T4. The Temperature-Sensitive Mutant Protein Thr157 (Right Arrow) Ile
;
J.Mol.Biol. (1987)
Structure of Bacteriophage T4 Lysozyme Refined at 1.7 Angstroms Resolution
J.Mol.Biol. (1987)
;Temperature-Sensitive Mutations of Bacteriophage T4 Lysozyme Occur at Sites with Low Mobility and Low Solvent Accessibility in the Folded Protein
;
Biochemistry (1987)
Common Precursor of Lysozymes of Hen Egg-White and Bacteriophage T4
Nature (1981)
;Crystallographic Determination of the Mode of Binding of Oligosaccharides to T4 Bacteriophage Lysozyme. Implications for the Mechanism of Catalysis
;
J.Mol.Biol. (1981)
Relation between Hen Egg White Lysozyme and Bacteriophage T4 Lysozyme. Evolutionary Implications
J.Mol.Biol. (1981)
Structure of the Lysozyme from Bacteriophage T4, an Electron Density Map at 2.4 Angstroms Resolution
J.Mol.Biol. (1978)
Atomic Coordinates for T4 Phage Lysozyme
Biochem.Biophys.Res.Commun. (1977)
Comparison of the Predicted and Observed Secondary Structure of T4 Phage Lysozyme
Biochim.Biophys.Acta (1975)
The Three Dimensional Structure of the Lysozyme from Bacteriophage T4
Proc.Natl.Acad.Sci.USA (1974)
Crystallographic Data for Lysozyme from Bacteriophage T4
J.Mol.Biol. (1973)
The Structural and Thermodynamic Consequences of Burying a Charged Residue within the Hydrophobic Core of T4 Lysozyme
To be Published
;Multiple Stabilizing Alanine Replacements within Alpha-Helix 126-134 of T4 Lysozyme Have Independent, Additive Effects on Both Structure and Stability
;
To be Published
;Tolerance of T4 Lysozyme to Proline Substitutions within the Long Interdomain Alpha-Helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions
;
To be Published
;Tolerance of T4 Lysozyme to Multiple Xaa (Right Arrow) Ala Substitutions: A Polyalanine Alpha-Helix Containing Ten Consecutive Alanines
;
To be Published
