Výsledky vyhledávání - "E R, Goedken"

Native-state energetics of a thermostabilized variant of ribonuclease HI

Autor: E R, Goedken, S, Marqusee

Publikováno v: Journal of molecular biology. 314(4)

Escherichia coli RNase HI is a well-characterized model system for protein folding and stability. Controlling protein stability is critical for both natural proteins and for the development of engineered proteins that function under extreme condition

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0d5abb19865b93741405949c8fd9d837
https://pubmed.ncbi.nlm.nih.gov/11734003

Zobrazit plný text záznamu

The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds

Autor: E A, Toth, C, Worby, J E, Dixon, E R, Goedken, S, Marqusee, T O, Yeates

Publikováno v: Journal of molecular biology. 301(2)

Adenylosuccinate lyase catalyzes two separate reactions in the de novo purine biosynthetic pathway. Through its dual action in this pathway, adenylosuccinate lyase plays an integral part in cellular replication and metabolism. Mutations in the human

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4266189ff07eeeea33f19fcd739ce572
https://pubmed.ncbi.nlm.nih.gov/10926519

Zobrazit plný text záznamu

Activation/attenuation model for RNase H. A one-metal mechanism with second-metal inhibition

Autor: J L, Keck, E R, Goedken, S, Marqusee

Publikováno v: The Journal of biological chemistry. 273(51)

Ribonucleases H (RNases H) comprise a family of metal-dependent enzymes that catalyze the hydrolysis of the 3'-O---P bond of RNA in RNA.DNA hybrids. The mechanism by which RNases H use active-site metal(s) for catalysis is unclear. Based upon the see

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::42e6f1b68e9e3ccf6fbcc9a4f98ce56a
https://pubmed.ncbi.nlm.nih.gov/9852071

Zobrazit plný text záznamu

Folding the ribonuclease H domain of Moloney murine leukemia virus reverse transcriptase requires metal binding or a short N-terminal extension

Autor: E R, Goedken, S, Marqusee

Publikováno v: Proteins. 33(1)

Reverse transcriptase (RT) is a modular enzyme carrying polymerase and ribonuclease H (RNase H) activities in separable domains. Retroviral replication requires both of these activities. The RNase H domain is responsible for hydrolysis of the RNA por

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9d465e4789f052fd2bc6d985370b889a
https://pubmed.ncbi.nlm.nih.gov/9741851

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání