Perturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties

Proteins: Structure, Function, and Bioinformatics

Volumn 15, Issue 4, 1993, Pages 401-412

  Pjura, Philip ^a   McIntosh, Lawrence P ^a,b   Wozniak, Joan A ^a   Matthews, Brian W ^a  

^a UNIVERSITY OF OREGON   (United States)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

fluorescence; phosphorescence; tryptophan

Indexed keywords

ALANINE; GLUTAMIC ACID; GLUTAMINE; GLYCINE; LYSOZYME; MUTANT PROTEIN; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIOPHAGE T4; CRYSTALLOGRAPHY; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE; PKA; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; SPECTROSCOPY;

BACTERIOPHAGE T4; CRYSTALLOGRAPHY; FLUORESCENCE POLARIZATION; GLUTAMINE; MAGNETIC RESONANCE SPECTROSCOPY; MERCAPTOETHANOL; MODELS, MOLECULAR; MURAMIDASE; MUTATION; PROTEIN CONFORMATION; SOLUBILITY; SPECTROMETRY, FLUORESCENCE; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; THERMODYNAMICS; TRYPTOPHAN;

EID: 0027406407     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.340150407     Document Type: Article

References (31)

1. Structure of lysozyme from bacteriophage T4: An electron density map at 2.4 Å resolution
2. Temperature‐sensitive mutations of bacteriophage T4 lysozyme occur at sites of low mobility and low solvent accessibility in the folded protein
3. Fluorescence and molecular dynamics study of the internal motion of the buried tryp‐tophan in bacteriophage T4 lysozyme: Effects of temperature and alteration of nonbended networks
4. Perturbation of tryptophan residues by point mutations in bacteriophage T4 lysozyme studied by optical detection of triplet‐state magnetic resonance spectroscopy
5. Oligonucleotide‐directed mutagenesis of DNA fragments cloned into M13 vectors
6. 15N labelling of proteins for proton and nitrogen‐15 NMR
7. Structure and thermal stability of phage T4 lysozyme
8. Structure of bacteriophage T4 lysozyme refined at 1.7 Å resolution
9. Comparison of the crystal structure of bacteriophage T4 lysozyme at low, medium and high ionic strengths
10. An efficient general‐purpose least‐squares refinement program for macromolecular structures
11. FRODO: A graphics fitting program for macromolecules
12. Thermal denaturation of bacteriophage T4 lysozyme at neutral pH
13. Purification of bacteriophage T4 lysozyme
14. 15NNMR resonances of bacteriophage T4 lysozyme
15. Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature sensitive mutant protein Thr 157 → Ile
16. 1H‐NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐H‐L‐Ala‐OH
17. The hydrogen bond in molecular recognition
18. Photophysics of tryptophan in bacteriophage T4 lysozymes
19. Mapping protein dynamics by X‐ray diffraction
20. Frameshift mutations and the genetic code
21. Structural studies of mutants of the lysozyme of bacteriophage T4. The temperature‐sensitive mutant protein Thr 157 → Ile
22. Crystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: Implications for the mechanism of catalysis
23. The influence of amino acid side‐chains on the free energy of helix‐coil transitions
24. pH‐induced denaturation of proteins: A single salt bridge contributes 3‐5 kcal/mol to the free energy of folding of T4 lysozyme
25. Enhanced protein thermostability from designed mutations that interact with alpha = helix dipoles
26. Conformation of amino acid side‐chains in proteins
27. A mutant T4 lysozyme (Val 131 → Ala) designed to increase thermostability by the reduction of strain within an α‐helix
28. Protein stability curves
29. The interpretation of protein structures: Estimation of static accessibility