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Folding of homologous proteins: conservation of the folding mechanism of the alpha subunit of tryptophan synthase from Escherichia coli, Salmonella typhimurium, and five interspecies hybrids.
Stackhouse TM, Onuffer JJ, Matthews CR, Ahmed SA, Miles EW. Stackhouse TM, et al. Biochemistry. 1988 Jan 26;27(2):824-32. doi: 10.1021/bi00402a050. Biochemistry. 1988. PMID: 3280027
The results show that all the proteins follow the same folding mechanism and are consistent with a previously proposed hypothesis [Hollecker, M., & Creighton, T. E. (1983) J. Mol. Biol. 168, 409; Krebs, H., Schmid, F. X., & Jaenicke, R. (1983) J. ...Analysis of the …
The results show that all the proteins follow the same folding mechanism and are consistent with a previously proposed hypothesis [Hollecker …
Release of the sigma subunit from Escherichia coli RNA polymerase transcription complexes is dependent on the promoter sequence.
Stackhouse TM, Telesnitsky AP, Meares CF. Stackhouse TM, et al. Biochemistry. 1989 Sep 19;28(19):7781-8. doi: 10.1021/bi00445a038. Biochemistry. 1989. PMID: 2482069
In order to study the position of sigma release, we have developed a method to quantify the photoaffinity labeling produced by an aryl azide positioned at the leading (5'-) end of nascent RNA, as a function of the transcript length [Stackhouse, T.M., & Meares, C …
In order to study the position of sigma release, we have developed a method to quantify the photoaffinity labeling produced by an aryl azide …
48 results