نتایج جستجو برای: s like rnase

تعداد نتایج: 1320013  

Journal: :The Journal of biological chemistry 1971
B Gutte R B Merrifield

A protected linear polypeptide of 124 amino acid residues with the sequence of bovine pancreatic ribonuclease A was synthesized by the solid phase method. The polypeptide was removed from the solid support and pursed, and the four disulfide bonds were closed by air oxidation of the reduced form. The synthetic enzyme was fractionated by gel filtration and ion exchange chromatography, and the mat...

2011
Martin Scholtz Edward A. Funkhouser Michael Douglas Daily

Local and Long-Range Electrostatic Interactions in Denatured Ribonuclease Sa: Comparing the Denatured Protein with Model Peptides (April 2002) Michael Douglas Daily Department of Biochemistry and Biophysics Texas A&M University Fellows Advisor: Dr. J. Martin Scholtz Department of Biochemistry and Biophysics The folding ol'proteins into three-dimensional, biologically active conformations demand...

Journal: :The Plant cell 1996
J. Murfett T. J. Strabala D. M. Zurek B. Mou B. Beecher B. A. McClure

In self-incompatible (SI) plants, the S locus acts to prevent growth of self-pollen and thus promotes outcrossing within the species. Interspecific crosses between SI and self-compatible (SC) species often show unilateral incompatibility that follows the SI x SC rule: SI species reject pollen from SC species, but the reciprocal crosses are usually compatible. The general validity of the SI x SC...

Journal: :Journal of Experimental Botany 2008
Elisabeth A. Mudd Stuart Sullivan Martin F. Gisby Aleksandr Mironov Chang Seob Kwon Won-Il Chung Anil Day

Endoribonuclease E (RNase E) is a regulator of global gene expression in Escherichia coli and is the best studied member of the RNase E/G ribonuclease family. Homologues are present in other bacteria but the roles of plant RNase E/G-like proteins are not known. Arabidopsis thaliana contains a single nuclear gene (At2g04270) encoding a product with the conserved catalytic domain of RNase E/G-lik...

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