Zobrazeno 1 - 10
of 209
pro vyhledávání: '"Julian M. Sturtevant"'
Publikováno v:
Journal of Molecular Biology. 283:155-177
We have recorded X-ray diffraction patterns at 3.1 A resolution from magnetically aligned fibres of the Pf3 strain of filamentous bacteriophage (Inovirus). The patterns are similar to patterns from the higher-temperature form of the Pf1 strain, indic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22c890781f77ce37de43ba2e4ebbd31f
https://doi.org/10.1006/jmbi.1998.2081
https://doi.org/10.1006/jmbi.1998.2081
Autor:
Julian M. Sturtevant
Publikováno v:
Chemistry and Physics of Lipids. 95:163-168
Differential scanning calorimetry is employed at a scan rate of 2 K h−1 to study the effects of sodium chloride and calcium chloride on the main phase transition of dilute aqueous suspensions of dimyristoylphosphatidylcholine. The primary effect of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6c9f94750079740ae27e771f06552d54
https://doi.org/10.1016/s0009-3084(98)00071-1
https://doi.org/10.1016/s0009-3084(98)00071-1
Publikováno v:
Protein Science. 7:961-965
Cytochrome b562 is a four-helix-bundle protein containing a non-covalently bound b-type heme prosthetic group. In the absence of heme, cytochrome b562 remains highly structured under native conditions. Here we report thermodynamic data for the therma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80530ec352a18b155bbc731221183e31
https://doi.org/10.1002/pro.5560070413
https://doi.org/10.1002/pro.5560070413
Autor:
John E. Ladbury, Ronan O'Brien, R. Wynn, Kevin W. Plaxco, B. Davis, Julian M. Sturtevant, Paul C. Driscoll
Publikováno v:
Protein Science. 6:1325-1332
The adaptability of Escherichia coli thioredoxin to the substitution of a series of non-natural amino acids has been investigated. Different thiosulfonated alkyl groups were inserted into the hydrophobic core of the protein in position 78 via disulfi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27dfad9717247879dc967b0f1e9f5e3c
https://doi.org/10.1002/pro.5560060621
https://doi.org/10.1002/pro.5560060621
Autor:
Yufeng Liu, Julian M. Sturtevant
Publikováno v:
Biophysical Chemistry. 64:121-126
The study of a wide variety of reversible reactions in solution indicates that the enthalpy, DeltaH(vH), which controls the temperature variation of the equilibrium constant for a reaction, can seldom, if ever, be taken to be independent of the tempe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::597ce6b0508e038dc841ccb23bd8699f
https://doi.org/10.1016/s0301-4622(96)02229-6
https://doi.org/10.1016/s0301-4622(96)02229-6
Autor:
Julian M. Sturtevant, Mary Munson, Karen G. Fleming, Suganthi Balasubramanian, Athena D. Nagi, Ronan O'Brien, Lynne Regan
Publikováno v:
Protein Science. 5:1584-1593
Here we describe how the systematic redesign of a protein's hydrophobic core alters its structure and stability. We have repacked the hydrophobic core of the four-helix-bundle protein, Rop, with altered packing patterns and various side chain shapes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34e68f06723e937bbefe794b494c357a
https://doi.org/10.1002/pro.5560050813
https://doi.org/10.1002/pro.5560050813
Autor:
Valsan Mandiyan, Min Zhou, Julian M. Sturtevant, Joseph Schlessinger, Ben Margolis, Ronan O'Brien, Mark A. Lemmon
Publikováno v:
Journal of Biological Chemistry. 271:4770-4775
The N-terminal 200 amino acids of SHC constitute a unique phosphotyrosine (Tyr(P)) interaction (PI) domain that shows no significant sequence similarity to the other Tyr(P)-recognizing module, the SH2 domain. We describe the thermodynamic parameters
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5e8718950e45d3e0158cb29a9ebd5c3
https://doi.org/10.1074/jbc.271.9.4770
https://doi.org/10.1074/jbc.271.9.4770
Autor:
Julian M. Sturtevant
Publikováno v:
Protein Science. 5:391-394
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::813707f52852cd7935bae2736a7014b5
https://doi.org/10.1002/pro.5560050224
https://doi.org/10.1002/pro.5560050224
Autor:
Yufeng Liu, Julian M. Sturtevant
Publikováno v:
Biochemistry. 35:3059-3062
The apparent change in heat capacity, delta C(p), accompanying the thermally induced unfolding of lysozyme and of ribonuclease A was determined by means of differential scanning calorimetry in dilute aqueous buffer containing one of the following add
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86cf39b168303cf1d781a0bc946246c0
https://doi.org/10.1021/bi952198j
https://doi.org/10.1021/bi952198j
Autor:
Julian M. Sturtevant, Song-Ja Bae
Publikováno v:
Biophysical Chemistry. 55:247-252
The thermal unfolding of eglin c, a small proteinase inhibitor of molecular weight 8.1 kDa, is studied by means of high sensitivity scanning calorimetry over a wide pH range in dilute buffer solutions, and in the presence of varying concentrations of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b416348934416e5c9ae0468c6412de9
https://doi.org/10.1016/0301-4622(94)00157-f
https://doi.org/10.1016/0301-4622(94)00157-f