Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering.
Biochemistry
(2002)
32
5145
(doi: 10.1021/bi00070a025)
Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing.
Biochemistry
(2002)
15
3342
(doi: 10.1021/bi00660a026)
Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
Biochemistry
(2002)
32
4322
(doi: 10.1021/bi00067a022)
ROLE OF PHENYLALANINE-327 IN THE CLOSURE OF LOOP-6 OF RIBULOSEBISPHOSPHATE CARBOXYLASE OXYGENASE FROM RHODOSPIRILLUM-RUBRUM
Biochemistry
(2002)
32
1940
(doi: 10.1021/bi00059a009)
Engineering a novel specificity in subtilisin BPN'.
Biochemistry
(2002)
32
1199
(doi: 10.1021/bi00056a001)
DETECTION OF AN INTERMEDIATE IN THE FOLDING OF THE (BETA-ALPHA)(8)-BARREL N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE FROM ESCHERICHIA-COLI
Biochemistry
(2002)
33
6350
(doi: 10.1021/bi00186a039)
Folding of subtilisin BPN': characterization of a folding intermediate.
Biochemistry
(2002)
32
18
(doi: 10.1021/bi00052a004)
Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles
Biochemistry
(2002)
29
9343
(doi: 10.1021/bi00492a006)
Nature and consequences of GroEL-protein interactions.
Biochemistry
(2002)
34
14581
(doi: 10.1021/bi00044a037)
Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy
Biochemistry
(2002)
33
8866
(doi: 10.1021/bi00196a003)
Movement of the Position of the Transition State in Protein Folding
Biochemistry
(2002)
34
13656
(doi: 10.1021/bi00041a047)
Structural factors contributing to the hydrophobic effect: the partly exposed hydrophobic minicore in chymotrypsin inhibitor 2.
Biochemistry
(2002)
34
13051
(doi: 10.1021/bi00040a016)
pKA Values of Carboxyl Groups in the Native and Denatured States of Barnase: The pKA Values of the Denatured State Are on Average 0.4 Units Lower Than Those of Model Compounds
Biochemistry
(2002)
34
9424
(doi: 10.1021/bi00029a018)
Rationally designing the accumulation of a folding intermediate of barnase by protein engineering.
Biochemistry
(2002)
32
13584
(doi: 10.1021/bi00212a026)
Natural variation of tyrosyl-tRNA synthetase and comparison with engineered mutants.
Biochemistry
(2002)
25
1887
(doi: 10.1021/bi00356a008)
Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase.
Biochemistry
(2002)
34
9288
(doi: 10.1021/bi00029a003)
Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: observation of Hammond behavior for the gross structure of the transition state and anti-Hammond behavior for structural elements for unfolding/folding of barnase.
Biochemistry
(2002)
34
6805
(doi: 10.1021/bi00020a027)
Probing the limits of protein-amino acid side chain recognition with the aminoacyl-tRNA synthetases. Discrimination against phenylalanine by tyrosyl-tRNA synthetases.
Biochemistry
(2002)
19
5520
(doi: 10.1021/bi00565a009)
Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea.
Biochemistry
(2002)
34
6795
(doi: 10.1021/bi00020a026)
