Stabilization of proteins by rational design of α-helix stability using helix/coil transition theory

1992 Serrano, 1993, The step-wise mutation of barnase to binase and a procedure for engineering increased stability of proteins: an experimental analysis of the evolution of protein stability, J. Mol. Biol, 233, 305, 10.1006/jmbi.1993.1508 Lee, 1991, Accurate prediction of the stability and activity effects of site-directed mutagenesis on a protein core, Nature, 352, 448, 10.1038/352448a0 Simonson, 1992, Thermodynamics of protein–peptide interactions in the ribonuclease S-system studied by molecular dynamics and free energy calculation, Biochemistry, 31, 8661, 10.1021/bi00151a037 Van Gunsteren, 1992, Prediction of the activity and stability effects of site-directed mutagenesis on a protein core, J. Mol. Biol, 227, 389, 10.1016/0022-2836(92)90895-Q Pickett, 1993, Empirical scale of side-chain conformational entropy in protein folding, J. Mol. Biol, 231, 825, 10.1006/jmbi.1993.1329 Totrov, 1992, Detailedab initio prediction of lysozyme–antibody complex with 1.6 å accuracy, Nature Struct. Biol, 1, 259, 10.1038/nsb0494-259 De Filippis, 1994, Predicting local structural changes that result from point mutations, Prot. Eng, 7, 1203, 10.1093/protein/7.10.1203 Lee, 1994, Predicting protein mutant energetics by self-consistent ensemble optimization, J. Mol. Biol, 236, 918, 10.1006/jmbi.1994.1198 Pielak, 1995, Protein thermal denaturation. Side-chain models and evolution: amino acid substitutions at a conserved helix–helix interface, Biochemistry, 34, 3268, 10.1021/bi00010a017 Chakrabartty, 1995, Stability ofα-helices, Adv. Prot. Chem, 46, 141, 10.1016/S0065-3233(08)60334-4 Serrano, 1989, Capping andα-helix stability, Nature, 342, 296, 10.1038/342296a0 Nicholson, 1991, Analysis of the interaction between charged side chains and theα-helix dipole using designed thermostable mutants of phage T4 lysozyme, Biochemistry, 30, 9816, 10.1021/bi00105a002 Horovitz, 1992, α-Helix stability in proteins. II. Factors that influence stability at an internal position, J. Mol. Biol, 227, 560, 10.1016/0022-2836(92)90907-2 Serrano, 1992, α-Helix stability in proteins. I. Empirical correlations concerning substitution of side chains at the N-  and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces, J. Mol. Biol, 227, 544, 10.1016/0022-2836(92)90906-Z Sancho, 1992, Histidine residues at the N-  and C-termini ofα-helices: perturbed pKas and protein stability, Biochemistry, 31, 2253, 10.1021/bi00123a006 Blaber, 1993, Structural basis of amino acidα-helix propensity, Science, 260, 1637, 10.1126/science.8503008 Muñoz, 1995, Elucidating the folding problem of helical peptides using empirical parameters, II: helix macrodipole effects and rational modification of the helical content of natural peptides, J. Mol. Biol, 245, 275, 10.1006/jmbi.1994.0023 Muñoz, 1995, Elucidating the folding problem of helical peptides using empirical parameters. III: Temperature and pH dependence, J. Mol. Biol, 245, 297, 10.1006/jmbi.1994.0024 Vendrell, 1991, Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity, EMBO J, 10, 11, 10.1002/j.1460-2075.1991.tb07915.x Coll, 1991, The NMR structure of the activation domain isolated from procarboxypeptidase B, EMBO J, 10, 1, 10.1002/j.1460-2075.1991.tb07914.x Guasch, 1992, Three dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation, J. Mol. Biol, 224, 141, 10.1016/0022-2836(92)90581-4 Catasús, 1995, The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis and 3D model, J. Biol. Chem, 270, 6651, 10.1074/jbc.270.12.6651 Villegas, 1995, Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2, Biochemistry, 10.1021/bi00046a017 Sanchez-Ruiz, 1988, Analysis of the thermal unfolding of porcine procarboxypeptidase A and its functional process by DSC, Eur. J. Biochem, 176, 225, 10.1111/j.1432-1033.1988.tb14272.x Conejero-Lara, 1991, DSC study of carboxypeptidase B, procarboxypeptidase B and its activation domain, Eur. J. Biochem, 200, 663, 10.1111/j.1432-1033.1991.tb16230.x Chen, 1974, Determination of the helix andβ-form of proteins in aqueous solution by circular dichroism, Biochemistry, 13, 3350, 10.1021/bi00713a027 Johnson, 1995, Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea, Biochemistry, 34, 6795, 10.1021/bi00020a026 Gill, 1989, Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem, 182, 319, 10.1016/0003-2697(89)90602-7 Wüthrich, 1986 Kabsch, 1983, Dictionary of protein secondary structure, Biopolymers, 20, 1080 Merutka, 1995, Random-coil1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG, J. Biomol. NMR, 5, 14, 10.1007/BF00227466