Zobrazeno 1 - 10
of 33
pro vyhledávání: '"J. M. Scholtz"'
Publikováno v:
Protein Science. 4:936-944
Anomalous NMR behavior of the hydroxyl proton resonance for Ser 31 has been reported for histidine-containing protein (HPr) from two microorganisms: Escherichia coli and Staphylococcus aureus. The unusual slow exchange and chemical shift exhibited by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9a6f926fb31dd7c4a8421bf65b97d84
https://doi.org/10.1002/pro.5560040513
https://doi.org/10.1002/pro.5560040513
Publikováno v:
Journal of Molecular Biology. 300:1377-1387
The dimeric interface of the leucine zipper coiled coil from GCN4 has been used to probe the contributions of hydrophobic and hydrogen bonding interactions to protein stability. We have determined the energetics of placing Ile or Asn residues at four
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5b34f7293883d6004e124d08c84c9bfb
https://doi.org/10.1006/jmbi.2000.3936
https://doi.org/10.1006/jmbi.2000.3936
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
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
Autor:
Eric M Nicholson, J. M. Scholtz
Publikováno v:
Biochemistry. 35:11369-11378
The conformational stability of the histidine-containing phosphocarrier protein (HPr) from Escherichia coli has been determined using a combination of thermal unfolding and urea denaturation experiments. The analysis of the denaturation data provides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b9abe0b3cdff234575f402817c7d977
https://doi.org/10.1021/bi960863y
https://doi.org/10.1021/bi960863y
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d543b5a55fef4d506b4300f9c590a9e
https://doi.org/10.1002/pro.5560041020
https://doi.org/10.1002/pro.5560041020
Autor:
J. M. Scholtz
Publikováno v:
Protein Science. 4:35-43
The conformational stability of the histidine-containing phosphocarrier protein (HPr) from Bacillus subtilis has been determined using a combination of thermal unfolding and solvent denaturation experiments. The urea-induced denaturation of HPr was m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13a17350ee86d561d75191d17bd674bb
https://doi.org/10.1002/pro.5560040106
https://doi.org/10.1002/pro.5560040106
Publikováno v:
Biochemistry. 32:9668-9676
A single pair of Glu and Lys residues has been placed at four different spacings, and in both orientations, in an otherwise neutral alanineglutamine peptide helix, and the contribution to helix stability of the different Glu-Lys interactions has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87da9e332d4e5b35269f595054f48086
https://doi.org/10.1021/bi00088a019
https://doi.org/10.1021/bi00088a019
Autor:
Robert L. Baldwin, J. M. Scholtz
Publikováno v:
Biochemistry. 32:4604-4608
Perchlorate-denatured ribonuclease A (PDR) is known to show a circular dichroism (CD) spectrum suggestive of substantial secondary structure. Thus, PDR may be a molten globule form of ribonuclease A. We find that any secondary structure present in PD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e027f34539cdac42a09e70f35635c27
https://doi.org/10.1021/bi00068a017
https://doi.org/10.1021/bi00068a017