the structure by a process of crystallographic 
refinement. 
Drs. Keith Wilson and Lisa Shewchuk, and Dr. 
Richard Brennan in collaboration with Dr. Anthony 
Otsuka, have recently determined the three- 
dimensional structure of the biotin repressor from 
Escherichia coli. This DNA-binding protein is both 
an enzyme and a repressor of transcription. The 
structure includes a helix-turn-helix DNA-binding 
region and a separate domain containing the enzy- 
matic active site. 
Studies of protein stability and protein-DNA inter- 
action were supponed in part by grants from the 
National Institutes of Health. 
Dr. Matthews is also Professor of Physics at the 
University of Oregon, Eugene, and Adjunct Pro- 
fessor of Biochemistry and Molecular Biology at 
the Oregon Health Sciences University. 
Books and Chapters of Books 
Tronrud, D.E., Roderick, S.L., and Matthews, 
B.W. 1992. Structural basis for the action of ther- 
molysin. International Research Conference on 
Matrix Metallopeptidases, Destin, EL (Birkedal- 
Hansen, H., Ed.). No. 1, pp 107-111. 
Articles 
Bell, J.A., Becktel, W.J., Sauer, U., Baase, W.A., and 
Matthews, B.W. 1992. Dissection of helix cap- 
ping in T4 lysozyme by structural and thermody- 
namic analysis of six amino acid substitutions at 
Thr 59. Biochemistry 51:5590-5596. 
Dao-pin, S., Alber, T., Baase, W.A., Wozniak, J.A., 
and Matthews, B.W. 1991. Structural and ther- 
modynamic analysis of the packing of two a- 
helices in bacteriophage T4 lysozyme. /Afo/ Biol 
221:647-667. 
Dao-pin, S., Anderson, D.E., Baase, W.A., Dahlquist, 
F.W., and Matthews, B.W. 1991. Structural and 
thermodynamic consequences of burying a 
charged residue within the hydrophobic core of 
T4 lysozyme. Biochemistry 30:11521-11529- 
Dao-pin, S., Nicholson, H., Baase, W.A., Zhang, X.-J., 
Wozniak, J.A., and Matthews, B.W. 1 99 1 Struc 
tural and genetic analysis of electrostatic and 
other interactions in bacteriophage T4 lysozyme. 
Ciba Pound Symp 161:52-62. 
Dao-pin, S., Soderlind, E., Baase, W.A., Wozniak, 
J.A., Sauer, U., and Matthews, B.W. 1991. Cu- 
mulative site-directed charge-change replace- 
ments in bacteriophage T4 lysozyme suggest that 
long-range electrostatic interactions contribute 
little to protein stability. / Mol Biol 221:873- 
887. 
Eriksson, A.E., Baase, W.A., Wozniak, J.A., and 
Matthews, B.W. 1992. A cavity-containing mu- 
tant of T4 lysozyme is stabilized by buried ben- 
zene. Nature 355:371-373- 
Eriksson, A.E., Baase, W.A., Zhang, X.-J., Heinz, 
D.W., Blaber, M., Baldwin, E.P., and Matthews, 
B.W. 1992. Response of a protein structure to 
cavity-creating mutations and its relation to the 
hydrophobic effect. Science 255:178-183- 
Heinz, D.W., Baase, W A., and Matthews, B.W. 
1992. Folding and function of a T4 lysozyme con- 
taining 10 consecutive alanines illustrate the re- 
dundancy of information in an amino acid se- 
quence. Proc Natl Acad Sci USA 89:3751-3755. 
Hurley, J.H., Baase, W.A., and Matthews, B.W. 
1 992. Design and structural analysis of alternative 
hydrophobic core packing arrangements in bacte- 
riophage T4 lysozyme. / Mol Biol 224:1143- 
1159- 
Jacobson, R-, Matsumura, M-, Faber, H.R., and 
Matthews, B.W. 1992. Structure of a stabilizing 
disulfide bridge mutant that closes the active-site 
cleft of T4 lysozyme. Protein Sci 1:46-57. 
Jacobson, R.H., and Matthews, B.W. 1992. Crystal- 
lization of |8-galactosidase from Escherichia coli. 
fMol Biol 223:1177-1182. 
Matsumura, M., and Matthews, B.W. 1991 • Stabili- 
zation of functional proteins by introduction of 
multiple disulfide bonds. Methods Enzymol 
202:336-356. 
Matthews, B.W. 1992. Facile folding [review of 
Branden, C, and Tooze, J. Introduction to Pro- 
tein Science]. Protein Sci 1:187. 
Nicholson, H., Anderson, D.E., Dao-pin, S., and 
Matthews, B.W. 1991. Analysis of the interac- 
tion between charged side-chains and the a-helix 
dipole using designed thermostable mutants of 
phage T4 lysozyme. Biochemistry 30:9816- 
9828. 
Sauer, U.H., Dao-pin, S., and Matthews, B.W. 
1992. Tolerance of T4 lysozyme to proline substi- 
tutions within the long interdomain a-helix illus- 
trates the adaptability of proteins to potentially 
destabilizing lesions. / Biol Chem 267:2393- 
2399. 
Wilson, K.P., Malcolm, B.A., and Matthews, B.W. 
1992. Structural and thermodynamic analysis of 
compensating mutations within the core of 
chicken egg white lysozyme. / Biol Chem 
267:10842-10849. 
Zhang, X.-J., Baase, W.A., and Matthews, B.W. 
1992. Multiple alanine replacements within a- 
helix 126-134 of T4 lysozyme have independent, 
additive effects on both structure and stability. 
Protein Sci l-.lGl-lld. 
STRUCTURAL BIOLOGY 479 
