Zobrazeno 1 - 10
of 199
pro vyhledávání: '"Pace Cn"'
Autor:
D Schell, Douglas V. Laurents, Jorge Santoro, Pace Cn, Marta Bruix, Manuel Rico, José Manuel Pérez-Cañadillas
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 44:200-211
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9ce4ed1a422283870b31ba433562baac
https://doi.org/10.1002/prot.1085
https://doi.org/10.1002/prot.1085
Publikováno v:
Biochemistry. 38:13379-13384
The side-chain carboxyl of Asp 76 in ribonuclease T1 (RNase T1) is buried, charged, non-ion-paired, and forms three good intramolecular hydrogen bonds (2.63, 2.69, and 2.89 A) and a 2.66 A hydrogen bond to a buried, conserved water molecule. When Asp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8cb4070865ba367136f5acc00184de2
https://doi.org/10.1021/bi991422s
https://doi.org/10.1021/bi991422s
Publikováno v:
Protein Science. 7:383-388
Trifluoroethanol (TFE) is often used to increase the helicity of peptides to make them usable as models of helices in proteins. We have measured helix propensities for all 20 amino acids in water and two concentrations of trifluoroethanol, 15 and 40%
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07903bd7b82a11e80653a71ff7b92664
https://doi.org/10.1002/pro.5560070219
https://doi.org/10.1002/pro.5560070219
Publikováno v:
Biochemistry. 36:14366-14374
Organophosphorus hydrolase (OPH, EC 8.1.3.1) is a homodimeric enzyme that catalyzes the hydrolysis of organophosphorus pesticides and nerve agents. We have analyzed the urea- and guanidinium chloride-induced equilibrium unfolding of OPH as monitored
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::854f04b821460ddf2116ec076f2f52d4
https://doi.org/10.1021/bi971596e
https://doi.org/10.1021/bi971596e
Autor:
Pace Cn, S Garcia, Gerald R. Grimsley, Jozef Sevcik, V Both, Robert W. Hartley, D Schell, E J Hebert, G Horn
Publikováno v:
Protein Expression and Purification. 11:162-168
The genes for three small ribonucleases from different strains of Streptomyces aureofaciens have been cloned and expressed in Escherichia coli. The purification of these ribonucleases from the periplasmic space is described. The yields range from 10
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dc4c56fa4242c0531044bc250fe621b
https://doi.org/10.1006/prep.1997.0776
https://doi.org/10.1006/prep.1997.0776
Publikováno v:
Biochemistry. 36:10923-10929
Our understanding of the factors stabilizing alpha-helical structure has been greatly enhanced by the study of model alpha-helical peptides. However, the relationship of these results to the folding of helices in intact proteins is not well character
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44fae8f966170fa04f792f74364aecbf
https://doi.org/10.1021/bi9707180
https://doi.org/10.1021/bi9707180
Publikováno v:
Nature Structural Biology. 6:910-912
Measuring protein conformational stability is one key to solving the protein folding problem. The conformational stability is the free energy change of the unfolding reaction, F ↔ U, under ambient conditions, ΔGU = GU - GF. Traditional methods of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ebe7431a61ded7769a51bb042d658247
https://doi.org/10.1038/13273
https://doi.org/10.1038/13273
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
Autor:
Pace Cn
Publikováno v:
Biochemistry. 40(2)
On the basis of studies of Asn to Ala mutants, the gain in stability from burying amide groups that are hydrogen bonded to peptide groups is 80 cal/(mol A(3)). On the basis of similar studies of Leu to Ala and Ile to Val mutants, the gain in stabilit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63545d623b3f64d6ed5284878c7c23f7
https://pubmed.ncbi.nlm.nih.gov/11148023
https://pubmed.ncbi.nlm.nih.gov/11148023
Autor:
J. M. Scholtz, Gerald R. Grimsley, Beatrice M. P. Huyghues-Despointes, L. R. Fee, Roy W. Alston, Pace Cn, Richard L. Thurlkill, Kevin L. Shaw
Publikováno v:
Protein science : a publication of the Protein Society. 8(9)
It is difficult to increase protein stability by adding hydrogen bonds or burying nonpolar surface. The results described here show that reversing the charge on a side chain on the surface of a protein is a useful way of increasing stability. Ribonuc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67ef9b86e71629e34eb90662f0f78248
https://pubmed.ncbi.nlm.nih.gov/10493585
https://pubmed.ncbi.nlm.nih.gov/10493585