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Found 15 results
Filters: keyword is Amino Acid Substitution [Clear All Filters]
2007
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2007. The crystal structure of phenylpyruvate decarboxylase from Azospirillum brasilense at 1.5 A resolution. Implications for its catalytic and regulatory mechanism.
FEBS J. 274(9):2363-2375. Abstract
2005
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2005. Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.
Nature. 346(3):773-788. Abstract
2003
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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
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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
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2002. Enzyme-substrate interactions in the purine-specific nucleoside hydrolase from Trypanosoma vivax.
J. Biol. Chem. 277(18):15938-15946. Abstract
2001
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2001. Hydrophobic core manipulations in ribonuclease T1.
Biochemistry. 40(34):10140-10149. Abstract
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2001. Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus.
309(1):193-201. Abstract
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2001. Deciphering the mechanism of RNase T1.
341:305-323.
2000
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2000. Thermodynamic analysis of helix-engineered forms of the activation domain of human procarboxypeptidase A2.
267(19):5891-5899. Abstract
1999
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1999. Hydrogen-exchange stabilities of RNase T1 and variants with buried and solvent-exposed Ala --> Gly mutations in the helix.
Biochemistry. 38(50):16481-16490. Abstract
1998
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1998. Crystallization of ccdB.
54(Pt 5):975-981. Abstract
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1998. An engineered ribonuclease preferring phosphorothioate RNA.
5(5):365-368. Abstract
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1998. Dissecting histidine interactions of ribonuclease T1 with asparagine and glutamine replacements: analysis of double mutant cycles at one position.
275(4):651-661. Abstract
1991
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1991. Subsite interactions of ribonuclease T1: Asn36 and Asn98 accelerate GpN transesterification through interactions with the leaving nucleoside N.
Biochemistry. 30(35):8666-8670. Abstract
1990
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1990. Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine.
Biochemistry. 29(38):9064-9072. Abstract