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Titolo:
The effect of net charge on the solubility, activity, and stability of ribonuclease Sa
Autore:
Shaw, KL; Grimsley, GR; Yakovlev, GI; Makarov, AA; Pace, CN;
Indirizzi:
Texas A&M Univ, Dept Med Biochem & Genet, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 Genet, College Stn, TX 77843 USA VA Engelhardt Mol Biol Inst, Moscow 119991, Russia VA Engelhardt Mol Biol Inst Moscow Russia 119991 , Moscow 119991, Russia Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 iophys, College Stn, TX 77843 USA Texas A&M Univ, Ctr Adv Biomol Res, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 ol Res, College Stn, TX 77843 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 6, volume: 10, anno: 2001,
pagine: 1206 - 1215
SICI:
0961-8368(200106)10:6<1206:TEONCO>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACILLUS-AMYLOLIQUEFACIENS BARNASE; PH-DEPENDENT STABILITY; CONFORMATIONAL STABILITY; PROTEIN STABILITY; DENATURED STATE; ELECTROSTATIC INTERACTIONS; BACTERIOPHAGE-T4 LYSOZYME; RECOMBINANT RIBONUCLEASE; GUANIDINE-HYDROCHLORIDE; HISTIDINE-RESIDUES;
Keywords:
ribonuclease Sa; isoelectric pH; net charge; electrostatic interactions; protein solubility; enzyme activity; protein stability;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Pace, CN Texas A&M Univ, Dept Med Biochem & Genet, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 ollege Stn, TX 77843 USA
Citazione:
K.L. Shaw et al., "The effect of net charge on the solubility, activity, and stability of ribonuclease Sa", PROTEIN SCI, 10(6), 2001, pp. 1206-1215

Abstract

The net charge and isoelectric pH (pI) of a protein depend on the content of ionizable groups and their pK values. Ribonuclease Sa (RNase Sa) is an acidic protein with a pI = 3.5 that contains no Lys residues. By replacing Asp and Glu residues on the surface of RNase Sa with Lys residues: we have created a 3K variant (D1K, D17K, E41K) with a pI = 6.4 and a 5K variant (3K D25K, E74K) with a pI = 10.2. We show that pi values estimated using pK values based on model compound data can be in error by >1 pH unit, and suggest how the estimation can be improved. For RNase Sa and the 3K and 5K variants, the solubility, activity, and stability have been measured as a function of pH. We find that the pH of minimum solubility varies with the pi of the protein, but that the pH of maximum activity and the pH of maximum stability do not.

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Documento generato il 29/03/20 alle ore 18:20:30