Zobrazeno 1 - 10
of 39
pro vyhledávání: '"C N, Pace"'
Publikováno v:
Molecular Biology. 49:933-938
Autor:
Andreas Koschinski, Vladimir A. Mitkevich, C. N. Pace, Alexander A. Makarov, Olga N. Ilinskaya
Publikováno v:
Молекулярная биология. 49:1041-1047
Bacterial ribonucleases (RNases) are considered to be potential anticancer agents. One of most important determinants of RNase cytotoxicity is the net charge of the molecule. In this work a set of mutants of the RNase from Streptomyces aureofaciens (
Publikováno v:
Molekuliarnaia biologiia. 49(6)
Bacterial ribonucleases (RNases) are considered to be potential anticancer agents. One of most important determinants of RNase cytotoxicity is the net charge of the molecule. In this work a set of mutants of the RNase from Streptomyces aureofaciens (
Publikováno v:
The FASEB Journal. 10:75-83
For 35 years, the prevailing view has been that the hydrophobic effect is the dominant force in protein folding. The importance of hydrogen bonding was always clear, but whether it made a net favorable contribution to protein stability was not. Studi
Publikováno v:
Protein Science. 4:2411-2423
The molar absorption coefficient, epsilon, of a protein is usually based on concentrations measured by dry weight, nitrogen, or amino acid analysis. The studies reported here suggest that the Edelhoch method is the best method for measuring epsilon f
Publikováno v:
Protein Science. 4:2138-2148
Denaturant m values, the dependence of the free energy of unfolding on denaturant concentration, have been collected for a large set of proteins. The m value correlates very strongly with the amount of protein surface exposed to solvent upon unfoldin
Publikováno v:
Biochemistry. 32:6152-6156
The rate of hydrogen bond formation at individual amino acid residues in ribonuclease T1 (RNase T1) has been investigated by the hydrogen-deuterium exchange-2D NMR (HDEx-2D NMR) technique (Udgaonkar & Baldwin, 1988; Rder et al., 1988) to gain insight
Publikováno v:
ChemInform. 22
Publikováno v:
Proteins. 44(3)
We have used NMR methods to characterize the structure and dynamics of ribonuclease Sa in solution. The solution structure of RNase Sa was obtained using the distance constraints provided by 2,276 NOEs and the C6-C96 disulfide bond. The 40 resulting
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 168