Transient folding intermediates characterized by protein engineering.
Nature
(1990)
346
440
(doi: 10.1038/346440a0)
Protein engineering and the study of structure—function relationships in receptors
Trends Pharmacol Sci
(1990)
11
280
(doi: 10.1016/0165-6147(90)90009-W)
Mapping the transition state and pathway of protein folding by protein engineering.
Nature
(1989)
340
122
(doi: 10.1038/340122a0)
Can a simple function for the dielectric response model electrostatic effects in globular proteins?
"Protein Engineering, Design and Selection"
(1989)
2
527
(doi: 10.1093/protein/2.7.527)
Stabilization of protein structure by interaction of α-helix dipole with a charged side chain
Nature
(1988)
335
740
(doi: 10.1038/335740a0)
TYROSYL-TRANSFER RNA-SYNTHETASE ACTS AS AN ASYMMETRIC DIMER IN CHARGING TRANSFER-RNA - A RATIONALE FOR HALF-OF-THE-SITES ACTIVITY
BIOCHEMISTRY-US
(1988)
27
5525
(doi: 10.1021/bi00415a021)
Contribution of hydrophobic interactions to protein stability.
Nature
(1988)
333
784
(doi: 10.1038/333784a0)
DISSECTION OF ENZYME STRUCTURE AND ACTIVITY
BIOLOGICAL CHEMISTRY HOPPE-SEYLER
(1988)
369
199
ASYMMETRY OF TYROSYL-TRANSFER RNA-SYNTHETASE IN SOLUTION
BIOCHEMISTRY-US
(1988)
27
1041
(doi: 10.1021/bi00403a029)
ARTIFACTS IN THE APPLICATION OF LINEAR FREE-ENERGY ANALYSIS
PROTEIN ENG
(1987)
1
442
(doi: 10.1093/protein/1.6.442)
Prediction of electrostatic effects of engineering of protein charges.
Nature
(1987)
330
86
(doi: 10.1038/330086a0)
Rational modification of enzyme catalysis by engineering surface charge
Nature
(1987)
328
496
(doi: 10.1038/328496a0)
USING PROTEIN ENGINEERING TO UNDERSTAND CATALYTIC YIELD
PROTEIN ENG
(1987)
1
261
STRUCTURE-ACTIVITY-RELATIONSHIPS
PROTEIN ENGINEERING
(1987)
1
233
SUBUNIT INTERACTIONS IN TYROSYL TRANSFER-RNA SYNTHETASE
PROTEIN ENGINEERING
(1987)
1
248
SITE-DIRECTED MUTAGENESIS IN THE EFFECTOR SITE OF ESCHERICHIA-COLI PHOSPHOFRUCTOKINASE
PROTEIN ENG
(1987)
1
260
Conversion of allosteric inhibition to activation in phosphofructokinase by protein engineering.
Nature
(1987)
326
811
(doi: 10.1038/326811a0)
Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering.
J Mol Biol
(1987)
193
803
(doi: 10.1016/0022-2836(87)90360-3)
