Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar
FEBS Letters
(1993)
332
81
(doi: 10.1016/0014-5793(93)80489-H)
Identification of the barstar binding site of barnase by NMR spectroscopy and hydrogen-deuterium exchange
FEBS Letters
(1993)
331
165
(doi: 10.1016/0014-5793(93)80319-P)
Step-wise Mutation of Barnase to Binase
Journal of molecular biology
(1993)
233
305
(doi: 10.1006/jmbi.1993.1508)
Folding of Subtilisin BPN': Role of the Pro-sequence
Journal of molecular biology
(1993)
233
293
(doi: 10.1006/jmbi.1993.1507)
Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding.
Proceedings of the National Academy of Sciences of the United States of America
(1993)
90
7814
(doi: 10.1073/pnas.90.16.7814)
Long-Range Surface Charge-Charge Interactions in Proteins
J Mol Biol
(1993)
232
574
(doi: 10.1006/jmbi.1993.1412)
Principles of protein stability derived from protein engineering experiments
Current Opinion in Structural Biology
(1993)
3
75
(doi: 10.1016/0959-440X(93)90205-Y)
THE CONTRIBUTION OF INTRA-LOOP HYDROGEN-BONDS TO PROTEIN STABILITY REVEALED BY 2 MUTANT CRYSTAL-STRUCTURES OF BARNASE
PROTEIN ENG
(1993)
6
6
Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces.
Journal of Molecular Biology
(1992)
227
544
(doi: 10.1016/0022-2836(92)90906-Z)
Alpha-helix stability in proteins. II. Factors that influence stability at an internal position.
J Mol Biol
(1992)
227
560
(doi: 10.1016/0022-2836(92)90907-2)
GENETIC-ENGINEERING AND PHOTOSYNTHESIS
RECHERCHE
(1992)
23
1066
Effect of active site residues in barnase on activity and stability.
Journal of molecular biology
(1992)
225
585
(doi: 10.1016/0022-2836(92)90387-y)
Mutation of asparagine 111 of rubisco from Rhodospirillum rubrum alters the carboxylase/oxygenase specificity
Journal of molecular biology
(1992)
225
891
(doi: 10.1016/0022-2836(92)90408-C)
Co-operative interactions during protein folding
J Mol Biol
(1992)
224
733
(doi: 10.1016/0022-2836(92)90557-z)
Dissection of an enzyme by protein engineering. The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity.
Journal of molecular biology
(1992)
224
741
(doi: 10.1016/0022-2836(92)90558-2)
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
Journal of molecular biology
(1992)
224
749
(doi: 10.1016/0022-2836(92)90559-3)
Histidine-aromatic interactions in barnase Elevation of histidine pKa and contribution to protein stability
Journal of Molecular Biology
(1992)
224
759
(doi: 10.1016/0022-2836(92)90560-7)
