Literature DB >> 3405287

Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3.

M Matsumura1, W J Becktel, B W Matthews.   

Abstract

Replacing the isoleucine at amino-acid position three of bacteriophage T4 lysozyme causes changes in the thermodynamic stability of the protein that are directly related to the hydrophobicity of the substituted residue. Structural analysis confirms that the hydrophobic stabilization is proportional to the reduction of the surface area accessible to solvent on folding.

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Year:  1988        PMID： 3405287     DOI： 10.1038/334406a0

Source DB:  PubMed          Journal:  Nature        ISSN： 0028-0836            Impact factor:   49.962


  62 in total

1.  Stabilization of hen egg white lysozyme by a cavity-filling mutation.

Authors:  T Ohmura; T Ueda; K Ootsuka; M Saito; T Imoto
Journal:  Protein Sci       Date:  2001-02       Impact factor: 6.725

2.  Theoretical studies of the response of a protein structure to cavity-creating mutations.

Authors:  J Lee; K Lee; S Shin
Journal:  Biophys J       Date:  2000-04       Impact factor: 4.033

3.  Use of surface area computations to describe atom-atom interactions.

Authors:  X de La Cruz; M Calvo
Journal:  J Comput Aided Mol Des       Date:  2001-06       Impact factor: 3.686

4.  On hydrophobicity and conformational specificity in proteins.

Authors:  Erik Sandelin
Journal:  Biophys J       Date:  2004-01       Impact factor: 4.033

5.  Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability.

Authors:  Mats Sandgren; Peter J Gualfetti; Andrew Shaw; Laurie S Gross; Mae Saldajeno; Anthony G Day; T Alwyn Jones; Colin Mitchinson
Journal:  Protein Sci       Date:  2003-04       Impact factor: 6.725

6.  Interatomic potentials and solvation parameters from protein engineering data for buried residues.

Authors:  Andrei L Lomize; Mikhail Y Reibarkh; Irina D Pogozheva
Journal:  Protein Sci       Date:  2002-08       Impact factor: 6.725

7.  Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region.

Authors:  Angela M Bertagna; Doug Barrick
Journal:  Proc Natl Acad Sci U S A       Date:  2004-08-16       Impact factor: 11.205

Review 8.  Protein folding.

Authors:  T E Creighton
Journal:  Biochem J       Date:  1990-08-15       Impact factor: 3.857

9.  Stability of mutant actins.

Authors:  D R Drummond; E S Hennessey; J C Sparrow
Journal:  Biochem J       Date:  1991-02-15       Impact factor: 3.857

10.  Synthesis of an enzymatically active FLP recombinase in vitro: search for a DNA-binding domain.

Authors:  A A Amin; P D Sadowski
Journal:  Mol Cell Biol       Date:  1989-05       Impact factor: 4.272
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