نتایج جستجو برای: s rnase

تعداد نتایج: 718068  

Journal: :Biochemistry 2003
Chiwook Park Ronald T Raines

The value of k(cat)/K(M) for catalysis of RNA cleavage by ribonuclease (RNase) A can exceed 10(9) M(-1) s(-1) in a solution of low salt concentration. This value approaches that expected for the diffusional encounter of the enzyme and its substrate. To reveal the physicochemical constraints upon catalysis by RNase A, the effects of salt concentration, pH, solvent isotope, and solvent viscosity ...

Journal: :The EMBO journal 1997
B Dichtl D Tollervey

RNase MRP is a ribonucleoprotein (RNP) particle which is involved in the processing of pre-rRNA at site A3 in internal transcribed spacer 1. Although RNase MRP has been analysed functionally, the structure and composition of the particle are not well characterized. A genetic screen for mutants which are synthetically lethal (sl) with a temperature-sensitive (ts) mutation in the RNA component of...

Journal: :Journal of plant physiology 2011
Melissa S Hillwig Charles Kanobe Robert W Thornburg Gustavo C Macintosh

Previous SDS PAGE gel analysis of the floral nectars from petunia and tobacco plants revealed significant differences in the protein patterns. Petunia floral nectar was shown to contain a number of RNase activities by in gel RNase activity assay. To identify these proteins in more detail, the bands with RNase activity were excised from gel and subjected to trypsin digestion followed by LC-MS/MS...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1993
D Suckau Y Shi S C Beu M W Senko J P Quinn F M Wampler F W McLafferty

For further insight into the role of solvent in protein conformer stabilization, the structural and dynamic properties of protein ions in vacuo have been probed by hydrogen-deuterium exchange in a Fourier-transform mass spectrometer. Multiply charged ions generated by electrospray ionization of five proteins show exchange reactions with 2H2O at 10(-7) torr (1 torr = 133.3 Pa) exhibiting pseudo-...

Journal: :The Plant cell 2008
Ed Newbigin Timothy Paape Joshua R Kohn

Many plants have a genetically determined self-incompatibility system in which the rejection of self pollen grains is controlled by alleles of an S locus. A common feature of these S loci is that separate pollen- and style-expressed genes (pollen S and style S, respectively) determine S allele identity. The long-held view has been that pollen S and style S must be a coevolving gene pair in orde...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1976
I Kandler-Singer K Kalthoff

In chironomid midges, the development of head and thorax in the embryo requires the function of cytoplasmic determinants localized near the anterior pole of the egg. Experimental inactivation of these determinants causes a dramatic switch in the developmental program of the embryo. Instead of the normal segment pattern, the aberrant pattern "double abdomen" is formed. Head, thorax, and anterior...

Journal: :Biopolymers 2007
J Kristin Smith John Hsieh Carol A Fierke

Ribonuclease P (RNase P) is a ribonucleoprotein (RNP) complex that catalyzes the metal-dependent maturation of the 5' end of precursor tRNAs (pre-tRNAs) in all organisms. RNase P is comprised of a catalytic RNA (P RNA), and at least one essential protein (P protein). Although P RNA is the catalytic subunit of the enzyme and is active in the absence of P protein under high salt concentrations in...

2015
Sanjeev Kumar V. Vernekar Zheng Liu Eva Nagy Lena Miller Karen A. Kirby Daniel J. Wilson Jayakanth Kankanala Stefan G. Sarafianos Michael A. Parniak Zhengqiang Wang

Reverse transcriptase (RT) associated ribonuclease H (RNase H) remains the only virally encoded enzymatic function not targeted by current chemotherapy against human immunodeficiency virus (HIV). Although numerous chemotypes have been reported to inhibit HIV RNase H biochemically, few show significant antiviral activity against HIV. We report herein the design, synthesis, and biological evaluat...

Journal: :The Journal of biological chemistry 1965
L M Sherwood J T Potts

Unfolding of the native conformation of pancreatic ribonuclease disrupts certain intramolecular associations of amino acids involving tyrosine residues (1) ; the subsequent absorbance changes serve as an index of the extent of denaturation of the enzyme (2). Of the 6 tyrosine residues of RNase A, 3 display distinct spectral properties which may be evaluated by determination of changes in ultrav...

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