Zobrazeno 1 - 10
of 54
pro vyhledávání: '"H.S. Subramanya"'
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Publikováno v:
Nucleic Acids Research. 26:2686-2693
PcrA from Bacillus stearothermophilus is a DNA helicase for which, despite the availability of a crystal structure, there is very little biochemical information. We show that the enzyme has a broad nucleotide specificity, even being able to hydrolyse
Publikováno v:
Current Opinion in Structural Biology. 8:14-18
The recent structure determinations of PcrA DNA helicase, NS3 RNA helicase, and Rep DNA helicase have revealed similarities between their folds. When these data are examined with sequence and biochemical analyses, as well as microscopy studies of hex
Publikováno v:
Nature. 384:379-383
THERE are a wide variety of helicases that unwind helical DNA1 and RNA substrates2. The twelve helicases that have been identified in Escherichia coli1 play a role in almost all cellular processes involving nucleic acids. We have solved the crystal s
Publikováno v:
Journal of Biological Chemistry. 271:11083-11089
The bacteriophage T7 DNA ligase gene was amplified using polymerase chain reaction-based methods and cloned into a T7 promoter-based expression vector. The protein was overexpressed to greater than 15% of total soluble protein and purified to homogen
Publikováno v:
Journal of Molecular Biology. 229:20-25
Sesbania mosaic virus (SMV) is a plant virus infecting Sesbania grandiflora plants in Andhra Pradesh, India. Amino acid sequence of the tryptic peptides of SMV coat protein were determined using a gas phase sequenator. These sequences showed identica
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Akademický článek
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Autor:
H.S. Subramanya, and N. Appaji Rao, V. Trivedi, V. Prakash, Venkatakrishna R. Jala, Handanahal S. Savithri, Siddegowda Bhavani, P. Kaul
Publikováno v:
IndraStra Global.
Serine hydroxymethyltransferase (SHMT), a pyridoxal 5'-phosphate (PLP)-dependent enzyme catalyzes the reversible conversion of L-Ser and tetrahydropteroylglutamate $(H_4PteGlu)$ to Gly and 5,10-methylene tetrahydropteroylglutamate $(CH_2-H_4PteGlu)$.
Publikováno v:
Biochemical and biophysical research communications. 288(4)
The CII protein of the temperate bacteriophage lambda is a transcriptional activator involved in the lysis-lysogeny switch of the phage. It is an unstable protein of 97 amino acids and is known to exist as a tetramer in the native state. The cII gene