MUTATIONAL STUDIES OF PROTEIN STRUCTURES AND THEIR STABILITIES

[1] EFFECTS OF SITE-SPECIFIC AMINO-ACID MODIFICATION ON PROTEIN INTERACTIONS AND BIOLOGICAL FUNCTION [J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1985, 54 : 597 - 629

[2] ACKERS GK, 1987, ANNU REV BIOPHYS BIO, V16, P583

[3] MOLECULAR CODE FOR COOPERATIVITY IN HEMOGLOBIN [J]. SCIENCE, 1992, 255 (5040) : 54 - 63

[4] EFFECTS OF POINT MUTATIONS IN A HINGE REGION ON THE STABILITY, FOLDING, AND ENZYMATIC-ACTIVITY OF ESCHERICHIA-COLI DIHYDROFOLATE-REDUCTASE [J]. BIOCHEMISTRY, 1991, 30 (31) : 7801 - 7809

[5] PROTEIN STABILITY AND ELECTROSTATIC INTERACTIONS BETWEEN SOLVENT EXPOSED CHARGED SIDE-CHAINS [J]. PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1990, 8 (01): : 23 - 29

[6] REPLACEMENTS OF PRO86 IN PHAGE-T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY [J]. SCIENCE, 1988, 239 (4840) : 631 - 635

[7] ALBER T, 1989, ANNU REV BIOCHEM, V58, P765, DOI 10.1146/annurev.biochem.58.1.765

[8] TEMPERATURE-SENSITIVE MUTATIONS OF BACTERIOPHAGE-T4 LYSOZYME OCCUR AT SITES WITH LOW MOBILITY AND LOW SOLVENT ACCESSIBILITY IN THE FOLDED PROTEIN [J]. BIOCHEMISTRY, 1987, 26 (13) : 3754 - 3758

[9] H-1-NMR EVIDENCE FOR 3 INTERCONVERTING FORMS OF STAPHYLOCOCCAL NUCLEASE - EFFECTS OF MUTATIONS AND SOLUTION CONDITIONS ON THEIR DISTRIBUTION [J]. BIOCHEMISTRY, 1989, 28 (01) : 204 - 211

[10] PH-INDUCED DENATURATION OF PROTEINS - A SINGLE SALT BRIDGE CONTRIBUTES 3-5 KCAL MOL TO THE FREE-ENERGY OF FOLDING OF T4-LYSOZYME [J]. BIOCHEMISTRY, 1990, 29 (09) : 2403 - 2408

[1] EFFECTS OF SITE-SPECIFIC AMINO-ACID MODIFICATION ON PROTEIN INTERACTIONS AND BIOLOGICAL FUNCTION [J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1985, 54 : 597 - 629

[2] ACKERS GK, 1987, ANNU REV BIOPHYS BIO, V16, P583

[3] MOLECULAR CODE FOR COOPERATIVITY IN HEMOGLOBIN [J]. SCIENCE, 1992, 255 (5040) : 54 - 63

[4] EFFECTS OF POINT MUTATIONS IN A HINGE REGION ON THE STABILITY, FOLDING, AND ENZYMATIC-ACTIVITY OF ESCHERICHIA-COLI DIHYDROFOLATE-REDUCTASE [J]. BIOCHEMISTRY, 1991, 30 (31) : 7801 - 7809

[5] PROTEIN STABILITY AND ELECTROSTATIC INTERACTIONS BETWEEN SOLVENT EXPOSED CHARGED SIDE-CHAINS [J]. PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1990, 8 (01): : 23 - 29

[6] REPLACEMENTS OF PRO86 IN PHAGE-T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY [J]. SCIENCE, 1988, 239 (4840) : 631 - 635

[7] ALBER T, 1989, ANNU REV BIOCHEM, V58, P765, DOI 10.1146/annurev.biochem.58.1.765

[8] TEMPERATURE-SENSITIVE MUTATIONS OF BACTERIOPHAGE-T4 LYSOZYME OCCUR AT SITES WITH LOW MOBILITY AND LOW SOLVENT ACCESSIBILITY IN THE FOLDED PROTEIN [J]. BIOCHEMISTRY, 1987, 26 (13) : 3754 - 3758

[9] H-1-NMR EVIDENCE FOR 3 INTERCONVERTING FORMS OF STAPHYLOCOCCAL NUCLEASE - EFFECTS OF MUTATIONS AND SOLUTION CONDITIONS ON THEIR DISTRIBUTION [J]. BIOCHEMISTRY, 1989, 28 (01) : 204 - 211

[10] PH-INDUCED DENATURATION OF PROTEINS - A SINGLE SALT BRIDGE CONTRIBUTES 3-5 KCAL MOL TO THE FREE-ENERGY OF FOLDING OF T4-LYSOZYME [J]. BIOCHEMISTRY, 1990, 29 (09) : 2403 - 2408