Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Upasana S. Potteth"'
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 91:108-120
Aromatic clusters in the core of proteins are often involved in imparting structural stability to proteins. However, their functional importance is not always clear. In this study, we investigate the thermosensing role of a phenylalanine cluster pres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72128dd8349a4d1d9fb697cf6d12e27a
https://doi.org/10.1002/prot.26414
https://doi.org/10.1002/prot.26414
Publikováno v:
Biochemistry. 60:1356-1367
In bacteria, the co-chaperone GrpE acts as a nucleotide exchange factor and plays an important role in controlling the chaperone cycle of DnaK. The functional form of GrpE is an asymmetric dimer, consisting of a non-ideal coiled coil. Partial unfoldi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::22ee87f0952c26aba923e354a95d261a
https://doi.org/10.1021/acs.biochem.1c00110
https://doi.org/10.1021/acs.biochem.1c00110
Autor:
Ravi Kumar, Shwetha Keshava, Dandamudi Usharani, Raja Narayanasamy, Anusree Lohithakshan, Upasana S. Potteth, Vibha Nagaraja
Publikováno v:
Biochimie. 182:217-227
Flavin adenine dinucleotide synthetase (FADS), a bifunctional prokaryotic enzyme, is involved in the synthesis of two vital cofactors, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD). Here, we investigated the biochemical characteri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a1a23255b2e06b29d296d8e06be7279
https://doi.org/10.1016/j.biochi.2021.01.013
https://doi.org/10.1016/j.biochi.2021.01.013
Publikováno v:
Biochemistry. 60(17)
In bacteria, the co-chaperone GrpE acts as a nucleotide exchange factor and plays an important role in controlling the chaperone cycle of DnaK. The functional form of GrpE is an asymmetric dimer, consisting of a non-ideal coiled coil. Partial unfoldi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a5add54730e5cea7f4de7e6adf87a458
https://pubmed.ncbi.nlm.nih.gov/33881310
https://pubmed.ncbi.nlm.nih.gov/33881310