The hydrogen bond in molecular recognition
Trends in Biochemical Sciences
(1987)
12
301
(doi: 10.1016/0968-0004(87)90146-0)
Concluding comment:–Fersht
Protein Engineering Design and Selection
(1987)
1
446
(doi: 10.1093/protein/1.6.446)
SINGLE-STRANDED M13 DNA - USE AS A CLONING VECTOR
Nucleic Acids Research
(1986)
14
10116
(doi: 10.1093/nar/14.24.10116)
Catalytic dissection of an enzyme active site
Biochemical Society Transactions
(1986)
14
1219
(doi: 10.1042/bst0141219)
Binding energy and catalysis: a lesson from protein engineering of the tyrosyl-tRNA synthetase
Trends in Biochemical Sciences
(1986)
11
321
(doi: 10.1016/0968-0004(86)90289-6)
Protein engineering of homodimeric tyrosyl-tRNA synthetase to produce active heterodimers.
J Biol Chem
(1986)
261
9576
Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships
Nature
(1986)
322
284
(doi: 10.1038/322284a0)
Structure and activity of the tyrosy1-tRNA synthetase: the hydrogen bond in catalysis and specificity
Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences
(1986)
317
305
(doi: 10.1098/rsta.1986.0041)
Molecular cloning of the gene encoding the valyl-tRNA synthetase from Bacillus stearothermophilus
Gene
(1986)
44
139
(doi: 10.1016/0378-1119(86)90053-3)
Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering.
Proc Natl Acad Sci U S A
(1985)
82
7840
(doi: 10.1073/pnas.82.23.7840)
Tailoring the pH dependence of enzyme catalysis using protein engineering
Nature
(1985)
318
375
(doi: 10.1038/318375a0)
Hydrogen bonding in enzymatic catalysis analysed by protein engineering
Nature
(1985)
316
656
(doi: 10.1038/316656a0)
Hydrogen bonding and biological specificity analysed by protein engineering.
Nature
(1985)
314
235
(doi: 10.1038/314235a0)
Synthesis of tetrahydrofolate derivatives.
Ciba Foundation symposium
(1985)
111
161
NAD+ degradation by resting cells.
Ciba Foundation symposium
(1985)
111
231
ENGINEERING OF TYROSYL TRANSFER-RNA SYNTHETASE
BIOCHIMIE
(1985)
67
737
The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus).
Cell
(1984)
38
835
(doi: 10.1016/0092-8674(84)90278-2)