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December 10, 1991Biochemistry

Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme

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Authors

SDS. DaopinHoward Hughes Medical InstituteDADavid E. AndersonUniversity of BernWBW.A. BaaseOregon State University

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Daopin et al. (1991) studied this question.

synapsesocial.com/papers/6a70b503a7fbea1e44082b2chttps://doi.org/10.1021/bi00113a006
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Second-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft1991 · 103 citations
  2. 2Genetic and structural analysis of the protein stability problem1987 · 227 citations
  3. 3pH-Induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme1990 · 523 citations
  4. 4Purification of Bacteriophage T4 Lysozyme1968 · 225 citations
  5. 5Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis1991 · 240 citations