You are here
Found 56 results
Filters: keyword is Muta [Clear All Filters]
2008
.
2008. Analysis of the thermodynamics of binding of an SH3 domain to proline-rich peptides using a chimeric fusion protein.
377(1):117-135. Abstract
2007
.
2007. Chloroplasts assemble the major subunit FaeG of Escherichia coli F4 (K88) fimbriae to strand-swapped dimers.
Journal Molecular Biology. 368(3):791-799. Abstract
.
2007. The conserved active site proline determines the reducing power of Staphylococcus aureus thioredoxin.
J. Mol. Biol.. 368(3):800-811. Abstract
.
2007. The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: understanding the determinants of binding affinity by comparison with Abl-SH3.
7:22. Abstract
2006
.
2006. Combining site-specific mutagenesis and seeding as a strategy to crystallize 'difficult' proteins: the case of Staphylococcus aureus thioredoxin.
Acta Crystallogr. Sect F Struct. Biol. Cryst. Commun.. 62(Pt 12):1255-1258. Abstract
.
2006. Comparative NMR study on the impact of point mutations on protein stability of Pseudomonas mendocina lipase.
15(8):1915-1927. Abstract
.
2006. Interplay between ion binding and catalysis in the thioredoxin-coupled arsenate reductase family.
J. Mol. Biol.. 360(4):826-838. Abstract
.
2006. Transition-state complex of the purine-specific nucleoside hydrolase of T. vivax: enzyme conformational changes and implications for catalysis.
Journal Molecular Biology. 359(2):331-346. Abstract
.
2006. The activation of electrophile, nucleophile and leaving group during the reaction catalysed by pI258 arsenate reductase.
Chembiochem.. 7(6):981-989. Abstract
2005
.
2005. Molecular basis of gyrase poisoning by the addiction toxin CcdB.
348(5):1091-1102. Abstract
.
2005. Pseudomonas aeruginosa lectin LecB is located in the outer membrane and is involved in biofilm formation.
151(Pt 5):1313-1323. Abstract
.
2005. Substrate-assisted leaving group activation in enzyme-catalyzed N-glycosidic bond cleavage.
J. Biol. Chem. 280(15):14799-14802. Abstract
.
2005. Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.
Nature. 346(3):773-788. Abstract
2004
.
2004. Structural basis of light chain amyloidogenicity: comparison of the thermodynamic properties, fibrillogenic potential and tertiary structural features of four Vlambda6 proteins.
17(4):323-331. Abstract
.
2004. How thioredoxin can reduce a buried disulphide bond.
J. Mol. Biol.. 339(3):527-537. Abstract
.
2004. The structure of a triple mutant of pI258 arsenate reductase from Staphylococcus aureus and its 5-thio-2-nitrobenzoic acid adduct.
Acta Crystallogr. D Biol. Crystallogr.. 60(Pt 6):1180-1184. Abstract
.
2004. Leaving group activation by aromatic stacking: an alternative to general acid catalysis.
J. Mol. Biol. 338(1):1-6. Abstract
2003
.
2003. Lack of negative charge in the E46Q mutant of photoactive yellow protein prevents partial unfolding of the blue-shifted intermediate.
42(49):14501-14506. Abstract
.
2003. Catalysis by nucleoside hydrolases.
Current opinion in structural biology. 13(6):731-738. Abstract
.
2003. A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme.
424(6950):783-788. Abstract
.
2003. Crystal structure of the intrinsically flexible addiction antidote MazE.
278(30):28252-28257. Abstract
.
2003. Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments.
330(2):397-407. Abstract
.
2003. Specific potassium binding stabilizes pI258 arsenate reductase from Staphylococcus aureus.
J. Biol. Chem.. 278(27):24673-24679. Abstract
.
2003. Characterization of single-tryptophan mutants of histidine-containing phosphocarrier protein: evidence for local rearrangements during folding from high concentrations of denaturant.
42(17):4883-4895. Abstract
2002
.
2002. All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade.
Proc. Natl. Acad. Sci. USA. 99(13):8506-8511. Abstract