Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Kevin L Shaw"'
Autor:
Vladimir A. Mitkevich, C. Nick Pace, Alexander A. Makarov, Olga N. Ilinskaya, Kevin L. Shaw, Florian Dreyer
Publikováno v:
Protein Science. 11:2522-2525
Ribonuclease Sa (pI = 3.5) from Streptomyces aureofaciens and its 3K (D1K, D17K, E41K) (pI = 6.4) and 5K (3K + D25K, E74K) (pI = 10.2) mutants were tested for cytotoxicity. The 5K mutant was cytotoxic to normal and v-ras-transformed NIH3T3 mouse fibr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd95c97a06e404c654697e54015ef2b0
https://doi.org/10.1110/ps.0216702
https://doi.org/10.1110/ps.0216702
Autor:
C. Nick Pace, Kevin L. Shaw
Publikováno v:
Proteins: Structure, Function, and Genetics. 41:1-7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cf4739f92273950d7ff41da0dd278f89
https://doi.org/10.1002/1097-0134(2000)41:4+<1::aid-prot10>3.0.co
https://doi.org/10.1002/1097-0134(2000)41:4+<1::aid-prot10>3.0.co
Publikováno v:
Protein Science. 9:1395-1398
Several recent studies have shown that it is possible to increase protein stability by improving electrostatic interactions among charged groups on the surface of the folded protein. However, the stability increases are considerably smaller than pred
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7e1d85b11257a6340a6f2d423f2f7ea
https://doi.org/10.1110/ps.9.7.1395
https://doi.org/10.1110/ps.9.7.1395
Autor:
E J Hebert, D Schell, Zbigniew Dauter, Keith S. Wilson, Gerald R. Grimsley, Kevin L. Shaw, V Both, Robert W. Hartley, Jozef Sevcik, Daniela Krajcikova, C.N. Pace
Publikováno v:
Journal of Molecular Biology. 279:271-286
Ribonucleases Sa, Sa2, and Sa3 are three small, extracellular enzymes produced by different strains of Streptomyces aureofaciens with amino acid sequences that are 50% identical. We have studied the unfolding of these enzymes by heat and urea to dete
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c7302c4825b1adbf17303bdb20f5f610
https://doi.org/10.1006/jmbi.1998.1760
https://doi.org/10.1006/jmbi.1998.1760
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 490
The stability of globular proteins is an important factor in determining their usefulness in basic research and medicine. A number of environmental factors contribute to the conformational stability of a protein, including pH, temperature, and ionic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::946f49776fcf066ebd9b0d4287e10b5e
https://pubmed.ncbi.nlm.nih.gov/19157078
https://pubmed.ncbi.nlm.nih.gov/19157078
Autor:
Vladimir A. Mitkevich, Kuppan Gokulan, James C. Sacchettini, J. Martin Scholtz, Saul R. Trevino, Richard L. Thurlkill, Stephanie Newsom, Kevin L. Shaw, Alexander A. Makarov, C. Nick Pace
Publikováno v:
Journal of molecular biology. 354(4)
The two most buried carboxyl groups in ribonuclease Sa (RNase Sa) are Asp33 (99% buried; pK 2.4) and Asp79 (85% buried; pK 7.4). Above these pK values, the stability of the D33A variant is 6kcal/mol less than wild-type RNase Sa, and the stability of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c58140d41e0ab2dcda95ec370aec573
https://pubmed.ncbi.nlm.nih.gov/16288913
https://pubmed.ncbi.nlm.nih.gov/16288913
Autor:
Saul R. Trevino, C. Nick Pace, Alexander A. Makarov, Gennady I. Yakovlev, Vladimir A. Mitkevich, Stephanie Newsom, Kevin L. Shaw
Publikováno v:
Protein science : a publication of the Protein Society. 12(10)
We have used site-specific mutagenesis to study the contribution of Glu 74 and the active site residues Gln 38, Glu 41, Glu 54, Arg 65, and His 85 to the catalytic activity and thermal stability of ribonuclease Sa. The activity of Gln38Ala is lowered
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5992d19b562744ea6361293d839aa69a
https://pubmed.ncbi.nlm.nih.gov/14500895
https://pubmed.ncbi.nlm.nih.gov/14500895
Autor:
C. Nick Pace, D Schell, James M. Briggs, Stephanie Newsom, Richard L. Thurlkill, Saul R. Trevino, Marta Bruix, Gerald R. Grimsley, Jan M. Antosiewicz, Kevin L. Shaw, Beatrice M. P. Huyghues-Despointes, Douglas V. Laurents, J. Martin Scholtz, Manuel Rico
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
instname
The pK values of the titratable groups in ribonuclease Sa (RNase Sa) (pI=3.5), and a charge-reversed variant with five carboxyl to lysine substitutions, 5K RNase Sa (pI=10.2), have been determined by NMR at 20 °C in 0.1 M NaCl. In RNase Sa, 18 pK va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13a612153c6170583190e7e3e5a5f02a
http://hdl.handle.net/10261/257802
http://hdl.handle.net/10261/257802
Autor:
Lubica Urbanikova, Pace Cn, J Bechert, E J Hebert, Jozef Sevcik, J M Scholtz, Kevin L. Shaw, G Horn
Publikováno v:
Journal of molecular biology. 312(2)
The aim of this study was to gain a better understanding of the contribution of hydrogen bonds by tyrosine -OH groups to protein stability. The amino acid sequences of RNases Sa and Sa3 are 69 % identical and each contains eight Tyr residues with sev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e91f2a3def2f20d7cdbe3a01bdcd689
https://pubmed.ncbi.nlm.nih.gov/11554795
https://pubmed.ncbi.nlm.nih.gov/11554795