242 related articles for article (PubMed ID: 11369859)
1. The effect of net charge on the solubility, activity, and stability of ribonuclease Sa.
Shaw KL; Grimsley GR; Yakovlev GI; Makarov AA; Pace CN
Protein Sci; 2001 Jun; 10(6):1206-15. PubMed ID: 11369859
[TBL] [Abstract][Full Text] [Related]
2. Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2).
Laurents DV; Huyghues-Despointes BM; Bruix M; Thurlkill RL; Schell D; Newsom S; Grimsley GR; Shaw KL; Treviño S; Rico M; Briggs JM; Antosiewicz JM; Scholtz JM; Pace CN
J Mol Biol; 2003 Jan; 325(5):1077-92. PubMed ID: 12527309
[TBL] [Abstract][Full Text] [Related]
3. Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic.
Ilinskaya ON; Dreyer F; Mitkevich VA; Shaw KL; Pace CN; Makarov AA
Protein Sci; 2002 Oct; 11(10):2522-5. PubMed ID: 12237473
[TBL] [Abstract][Full Text] [Related]
4. pK values of histidine residues in ribonuclease Sa: effect of salt and net charge.
Huyghues-Despointes BM; Thurlkill RL; Daily MD; Schell D; Briggs JM; Antosiewicz JM; Pace CN; Scholtz JM
J Mol Biol; 2003 Jan; 325(5):1093-105. PubMed ID: 12527310
[TBL] [Abstract][Full Text] [Related]
5. Contribution of active site residues to the activity and thermal stability of ribonuclease Sa.
Yakovlev GI; Mitkevich VA; Shaw KL; Trevino S; Newsom S; Pace CN; Makarov AA
Protein Sci; 2003 Oct; 12(10):2367-73. PubMed ID: 14500895
[TBL] [Abstract][Full Text] [Related]
6. Asp79 makes a large, unfavorable contribution to the stability of RNase Sa.
Trevino SR; Gokulan K; Newsom S; Thurlkill RL; Shaw KL; Mitkevich VA; Makarov AA; Sacchettini JC; Scholtz JM; Pace CN
J Mol Biol; 2005 Dec; 354(4):967-78. PubMed ID: 16288913
[TBL] [Abstract][Full Text] [Related]
7. The role of protein stability, solubility, and net charge in amyloid fibril formation.
Schmittschmitt JP; Scholtz JM
Protein Sci; 2003 Oct; 12(10):2374-8. PubMed ID: 14500896
[TBL] [Abstract][Full Text] [Related]
8. Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa.
Trevino SR; Scholtz JM; Pace CN
J Mol Biol; 2007 Feb; 366(2):449-60. PubMed ID: 17174328
[TBL] [Abstract][Full Text] [Related]
9. Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Laurents DV; Scholtz JM; Rico M; Pace CN; Bruix M
Biochemistry; 2005 May; 44(21):7644-55. PubMed ID: 15909979
[TBL] [Abstract][Full Text] [Related]
10. Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa.
Alston RW; Urbanikova L; Sevcik J; Lasagna M; Reinhart GD; Scholtz JM; Pace CN
Biophys J; 2004 Dec; 87(6):4036-47. PubMed ID: 15377518
[TBL] [Abstract][Full Text] [Related]
11. Conformational consequences of ionization of Lys, Asp, and Glu buried at position 66 in staphylococcal nuclease.
Karp DA; Stahley MR; García-Moreno B
Biochemistry; 2010 May; 49(19):4138-46. PubMed ID: 20329780
[TBL] [Abstract][Full Text] [Related]
12. Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.
Trefethen JM; Pace CN; Scholtz JM; Brems DN
Protein Sci; 2005 Jul; 14(7):1934-8. PubMed ID: 15937282
[TBL] [Abstract][Full Text] [Related]
13. Tyrosine hydrogen bonds make a large contribution to protein stability.
Pace CN; Horn G; Hebert EJ; Bechert J; Shaw K; Urbanikova L; Scholtz JM; Sevcik J
J Mol Biol; 2001 Sep; 312(2):393-404. PubMed ID: 11554795
[TBL] [Abstract][Full Text] [Related]
14. Residues involved in the catalysis, base specificity, and cytotoxicity of ribonuclease from Rana catesbeiana based upon mutagenesis and X-ray crystallography.
Leu YJ; Chern SS; Wang SC; Hsiao YY; Amiraslanov I; Liaw YC; Liao YD
J Biol Chem; 2003 Feb; 278(9):7300-9. PubMed ID: 12499382
[TBL] [Abstract][Full Text] [Related]
15. The role of acidic amino acid residues in the structural stability of snake cardiotoxins.
Chiang CM; Chang SL; Lin HJ; Wu WG
Biochemistry; 1996 Jul; 35(28):9177-86. PubMed ID: 8703923
[TBL] [Abstract][Full Text] [Related]
16. Experimental and theoretical study of electrostatic effects on the isoelectric pH and the pKa of the catalytic residue His-102 of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase).
Bastyns K; Froeyen M; Diaz JF; Volckaert G; Engelborghs Y
Proteins; 1996 Mar; 24(3):370-8. PubMed ID: 8778784
[TBL] [Abstract][Full Text] [Related]
17. Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3.
Pace CN; Hebert EJ; Shaw KL; Schell D; Both V; Krajcikova D; Sevcik J; Wilson KS; Dauter Z; Hartley RW; Grimsley GR
J Mol Biol; 1998 May; 279(1):271-86. PubMed ID: 9636716
[TBL] [Abstract][Full Text] [Related]
18. His...Asp catalytic dyad of ribonuclease A: conformational stability of the wild-type, D121N, D121A, and H119A enzymes.
Quirk DJ; Park C; Thompson JE; Raines RT
Biochemistry; 1998 Dec; 37(51):17958-64. PubMed ID: 9922164
[TBL] [Abstract][Full Text] [Related]
19. Influence of Glu/Arg, Asp/Arg, and Glu/Lys Salt Bridges on α-Helical Stability and Folding Kinetics.
Meuzelaar H; Vreede J; Woutersen S
Biophys J; 2016 Jun; 110(11):2328-2341. PubMed ID: 27276251
[TBL] [Abstract][Full Text] [Related]
20. Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1.
Hebert EJ; Giletto A; Sevcik J; Urbanikova L; Wilson KS; Dauter Z; Pace CN
Biochemistry; 1998 Nov; 37(46):16192-200. PubMed ID: 9819211
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
