메뉴 건너뛰기




Volumn 3, Issue 1, 1993, Pages 75-83

Principles of protein stability derived from protein engineering experiments

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AROMATIC AMINO ACID; HISTIDINE; PEPTIDE; PROTEIN; SYNTHETIC PEPTIDE;

EID: 0027462173     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0959-440X(93)90205-Y     Document Type: Article
Times cited : (270)

References (100)
  • 2
    • 0026556022 scopus 로고
    • On the Interpretation of Biochemical Data by Molecular Dynamics Computer Simulation
    • (1992) Eur J Biochem , vol.204 , pp. 947-961
    • Van Gunsteren1    Mark2
  • 3
    • 0024281312 scopus 로고
    • Relationships between Apparent Binding Energies Measured in Site-directed Mutagenesis Experiments and Energetics of Binding and Catalysis
    • (1988) Biochemistry , vol.27 , pp. 1577-1580
    • Fersht1
  • 5
    • 0026511656 scopus 로고
    • The Folding of an Enzyme. 1. Theory of Protein Engineering Analysis of Stability and Pathway of Protein Folding
    • (1992) J Mol Biol , vol.224 , pp. 771-782
    • Fersht1    Matouschek2    Serrano3
  • 8
    • 0024963569 scopus 로고
    • Residual Structure in Large Fragments of Staphylococcal Nuclease: Effects of Amino Acid Substitutions
    • (1989) Biochemistry , vol.28 , pp. 936-944
    • Shortle1    Meeker2
  • 11
    • 0027050824 scopus 로고
    • Modeling the Effects of Mutations on the Denatured States of Proteins
    • (1992) Protein Sci , vol.1 , pp. 201-215
    • Shortle1    Chan2    Dill3
  • 12
    • 0026602704 scopus 로고
    • Urea Denaturation of Barnase — pH Dependence and Characterization of the Unfolded State
    • (1992) Biochemistry , vol.31 , pp. 2728-2734
    • Pace1    Laurents2    Erickson3
  • 13
  • 14
  • 15
    • 0026209013 scopus 로고
    • The Helical S-constant for Alanine in Water Derived from Template-nucleated Helices
    • (1991) Nature , vol.352 , pp. 451-454
    • Kemp1    Boyd2    Muendel3
  • 17
    • 0026709329 scopus 로고
    • 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
    • (1992) J Mol Biol , vol.227 , pp. 544-549
    • Serrano1    Sancho2    Hirshberg3    Fersht4
  • 21
    • 0025222978 scopus 로고
    • A Thermodynamic Scale for the Helix-forming Tendencies of the Commonly Occurring Amino Acids
    • (1990) Science , vol.250 , pp. 646-651
    • Oneil1    Degrado2
  • 22
    • 0025260032 scopus 로고
    • Side Chain Contributions to the Stability of Alpha-helical Structure in Peptides
    • (1990) Science , vol.250 , pp. 669-673
    • Lyu1    Liff2    Marky3    Kallenbach4
  • 23
    • 0026253633 scopus 로고
    • The Helix-Coil Transition in Heterogeneous Peptides with Specific Side-chain Interactions — Theory and Comparison with CD Spectral Data
    • (1991) Biopolymers , vol.31 , pp. 1605-1614
    • Gans1    Lyu2    Manning3    Woody4    Kallenbach5
  • 25
    • 0026696173 scopus 로고
    • Dissection of Helix Capping in T4 Lysozyme by Structural and Thermodynamic Analysis of Six Amino Acid Substitutions at Thr 59
    • (1992) Biochemistry , vol.31 , pp. 3590-3596
    • Bell1    Becktel2    Sauer3    Baase4    Matthews5
  • 27
    • 0026010011 scopus 로고
    • Analysis of the Interaction Between Charged Side Chains and the Alpha-helix Dipole using Designed Thermostable Mutants of Phage T4-Lysozyme
    • (1991) Biochemistry , vol.30 , pp. 9816-9828
    • Nicholson1    Anderson2    Daopin3    Matthews4
  • 28
    • 0026590664 scopus 로고
    • Histidine Residues at the N-termini and C-termini of Alpha-helices—Perturbed pKas and Protein Stability
    • (1992) Biochemistry , vol.31 , pp. 2253-2258
    • Sancho1    Serrano2    Fersht3
  • 29
    • 0026674251 scopus 로고
    • Alpha-helix Stability in Proteins. II. Factors that Influence Stability at an Internal Position
    • (1992) J Mol Biol , vol.227 , pp. 560-568
    • Horovitz1    Matthews2    Fersht3
  • 30
    • 0026806846 scopus 로고
    • Tolerance of T4-Lysozyme to Proline Substitutions within the Long Interdomain Alpha-helix Illustrates the Adaptability of Proteins to Potentially Destabilizing Lesions
    • (1992) J Biol Chem , vol.267 , pp. 2393-2399
    • Sauer1    Sun2    Matthews3
  • 31
    • 0027093322 scopus 로고
    • Multiple Alanine Replacements within Alpha-helix-126–134 of T4 Lysozyme Have Independent, Additive Effects on Both Structure and Stability
    • (1992) Protein Sci , vol.1 , pp. 761-776
    • Zhang1    Baase2    Matthews3
  • 33
    • 0026665778 scopus 로고
    • Side-chain Entropy Opposes Alpha helix Formation but Rationalizes Experimentally Determined Helix-forming Propensities
    • 2nd Edn.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5937-5941
    • Creamer1    Rose2
  • 34
    • 0025767212 scopus 로고
    • Thermodynamics and Mechanism of Alpha Helix Initiation in Alanine and Valine Peptides
    • (1991) Biochemistry , vol.30 , pp. 6059-6070
    • Tobias1    Brooks2
  • 39
    • 0025327584 scopus 로고
    • Protein Stability and Electrostatic Interactions between Solvent Exposed Charged Side Chains
    • (1990) Proteins , vol.8 , pp. 23-29
    • Akke1    Forsen2
  • 41
    • 0025718955 scopus 로고
    • Contributions of Engineered Surface Salt Bridges to the Stability of T4 Lysozyme Determined by Directed Mutagenesis
    • (1991) Biochemistry , vol.30 , pp. 7142-7153
    • Dao-Pin1    Nicholson2    Matthews3
  • 42
    • 0026565486 scopus 로고
    • Energetic Contribution of Solvent-exposed Ion Pairs to Alpha-helix Structure
    • (1992) J Mol Biol , vol.223 , pp. 343-350
    • Lyu1    Gans2    Kallenbach3
  • 45
    • 0015505502 scopus 로고
    • Conformational Equilibria in α- and δ-Chymotrypsin. The Energetics and Importance of the Salt Bridge
    • (1972) J Mol Biol , vol.64 , pp. 497-509
    • Fersht1
  • 50
    • 0025234587 scopus 로고
    • pH-induced Denaturation of Proteins—a Single Salt Bridge Contributes 3–5 Kcal Mol to the Free Energy of Folding of T4-lysozyme
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson1    Becktel2    Dahlquist3
  • 51
    • 0022386437 scopus 로고
    • Tailoring the pH Dependence of Enzyme Catalysis by Protein Engineering
    • (1986) Nature , vol.318 , pp. 375-376
    • Thomas1    Russell2    Fersht3
  • 52
    • 0023646665 scopus 로고
    • Rational Modification of Enzyme Catalysis
    • (1987) Nature , vol.328 , pp. 496-500
    • Russell1    Fersht2
  • 53
    • 0023660015 scopus 로고
    • Electrostatic Effects on Modification of Charged Groups in the Active Site Cleft of Subtilisin by Protein Engineering
    • (1987) J Mol Biol , vol.193 , pp. 803-813
    • Russell1    Thomas2    Fersht3
  • 56
    • 0023280069 scopus 로고
    • Calculation of Electrostatic Potentials in an Enzyme Active Site
    • (1987) Nature , vol.330 , pp. 184-186
    • Gilson1    Honig2
  • 62
  • 63
    • 0017187836 scopus 로고
    • The Nature of the Accessible and Buried Surfaces in Proteins
    • (1976) J Mol Biol , vol.105 , pp. 1-14
    • Chothia1
  • 67
    • 0025005525 scopus 로고
    • Contributions of the Large Hydrophobic Amino Acids to the Stability of Staphylococcal Nuclease
    • (1990) Biochemistry , vol.29 , pp. 8033-8041
    • Shortle1    Sittes2    Meeker3
  • 70
    • 0023741058 scopus 로고
    • Hydrophobic Stabilization in T4 Lysozyme Determined Directly by Multiple Substitutions of Ile3
    • (1988) Nature , vol.344 , pp. 406-410
    • Matsumura1    Becktel2    Matthews3
  • 73
    • 0026766573 scopus 로고
    • Structural and Energetic Consequences of Disruptive Mutations in a Protein Core
    • (1992) Biochemistry , vol.31 , pp. 4324-4333
    • Ijm1    Farruggio2    Sauer3
  • 74
    • 0026532266 scopus 로고
    • Design in Structural Analysis of Alternative Hydrophobic Core Packing Arrangements in Bacteriophage T4 Lysozome
    • (1992) J Mol Biol , vol.224 , pp. 1143-1159
    • Hurley1    Baase2    Matthews3
  • 75
    • 0026210071 scopus 로고
    • Accurate Prediction of the Stability and Activity Effects of Site-directed Mutagenesis on a Protein Core
    • (1991) Nature , vol.352 , pp. 448-451
    • Lee1    Levitt2
  • 77
    • 0000299809 scopus 로고
    • Aromatic-Aromatic Interactions: Free Energy Profiles for the Benzene Dimer in Water, Chloroform, and Liquid Benzene
    • (1990) J Am Chem Soc , vol.112 , pp. 4768-4774
    • Jorgensen1    Severance2
  • 78
    • 0022419375 scopus 로고
    • Aromatic-Aromatic Interaction: a Mechanism of Protein Structure Stabilization
    • (1985) Science , vol.229 , pp. 23-28
    • Burley1    Petsko2
  • 79
    • 0342810084 scopus 로고
    • The Interaction between Phenylalanine Rings in Proteins
    • (1985) FEBS Lett , vol.191 , pp. 1-6
    • Singh1    Thornton2
  • 81
    • 0025878347 scopus 로고
    • π-π Interactions: the Geometry and Energetics of Phenylalanine-Phenylalanine Interactions in Proteins
    • (1991) J Mol Biol , vol.218 , pp. 837-846
    • Hunter1    Singh2    Thornton3
  • 82
    • 0025756736 scopus 로고
    • Aromatic Interactions and Protein Stability—Investigation by Double-mutant Cycles
    • (1991) J Mol Biol , vol.218 , pp. 465-475
    • Serrano1    Bycroft2    Fersht3
  • 86
    • 0014187163 scopus 로고
    • Fluorometric Detection of Histidine Tryptophan Complexes in Peptides and Proteins
    • (1967) Eur J Biochem , vol.3 , pp. 139-144
    • Shinitzky1    Goldman2
  • 87
    • 0023783477 scopus 로고
    • Conformational Stability and Activity of Ribonuclease T1 with Zero, One and Two Intact Disulphide Bonds
    • (1988) J Biol Chem , vol.263 , pp. 11820-11825
    • Pace1    Grimsley2    Thomson3    Barnett4
  • 88
    • 0022998684 scopus 로고
    • In vivo Formation and Stability of Engineered Disulfide Bonds in Subtilisin
    • (1986) J Biol Chem , vol.261 , pp. 6564-6670
    • Wells1    Powers2
  • 92
    • 0025307389 scopus 로고
    • Crystal Structures of Subtilisin BPN′ Variants Containing Disulfide Bonds and Cavities: Concerted Structural Arrangements Induced by Mutagenesis
    • (1990) Proteins , vol.7 , pp. 343-357
    • Katz1    Kossiakoff2
  • 93
    • 0023034995 scopus 로고
    • The Crystallographically Determined Structures of Atypical Strained Disulfides Engineered into Subtilisin
    • (1986) J Biol Chem , vol.261 , pp. 15480-15485
    • Katz1    Kossiakoff2
  • 94
    • 0023007337 scopus 로고
    • Computer-aided Model Building Strategies for Protein Design
    • (1986) Biochemistry , vol.25 , pp. 5987-5991
    • Pabo1    Suchanek2
  • 96
    • 0026055156 scopus 로고
    • Analysis of the Steric Strain in the Polypeptide Backbone of Protein Molecules
    • (1991) Proteins , vol.11 , pp. 223-229
    • Herzberg1    Moult2
  • 98
    • 0021504608 scopus 로고
    • The Use of Double Mutants to Detect Structural Changes in the Active Site of the Tyrosyl-tRNA Synthetase (Bacillus stearothermophilus
    • (1984) Cell , vol.38 , pp. 835-840
    • Carter1    Winter2    Wilkinson3    Fersht4
  • 99
    • 0025126043 scopus 로고
    • Strategy for Analysing the Cooperativity of Intramolecular Interactions in Peptides and Proteins
    • (1990) J Mol Biol , vol.214 , pp. 613-617
    • Horovitz1    Fersht2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.