Zobrazeno 1 - 10
of 25
pro vyhledávání: '"F. Walkenhorst"'
Autor:
William F. Walkenhorst
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1858:926-935
The increase in antibiotic resistant and multi-drug resistant bacterial infections has serious implications for the future of health care. The difficulty in finding both new microbial targets and new drugs against existing targets adds to the concern
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71e65ed5f11d86e6da638a8d852dfda2
https://doi.org/10.1016/j.bbamem.2015.12.034
https://doi.org/10.1016/j.bbamem.2015.12.034
Publikováno v:
Journal of the American Chemical Society. 131:7609-7617
We recently described ten peptides selected from a 16,384-member combinatorial library based on their ability to permeabilize synthetic lipid vesicles in vitro (Rathinakumar R and Wimley WC, J. Am. Chem. Soc. 2008, 130, 9849-9858). These peptides did
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bf52576370826c7a9873433d7ddb523
https://doi.org/10.1021/ja8093247
https://doi.org/10.1021/ja8093247
Publikováno v:
Protein Science. 11:82-91
Pulsed hydrogen exchange methods were used to follow the formation of structure during the refolding of acid-denatured staphylococcal nuclease containing a stabilizing Leu substitution at position 124 (H124L SNase). The protection of more than 60 bac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca8fd4c602e556e6bcbffd373e1a3245
https://doi.org/10.1110/ps.28202
https://doi.org/10.1110/ps.28202
Autor:
W. F. Walkenhorst
Publikováno v:
Protein Science. 11:82-91
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f9e414962f53074d9a4dee9241091de0
https://doi.org/10.1110/ps.ps.28202
https://doi.org/10.1110/ps.ps.28202
Publikováno v:
Biochemistry and Cell Biology. 79:349-363
The contribution of the linker region to maintenance of condensed chromatin was examined in two model systems, namely sea urchin sperm nuclei and chicken red blood cell nuclei. Linkerless nuclei, prepared by extensive digestion with micrococcal nucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b1fa127809756a3b27f55073c0770290
https://doi.org/10.1139/o01-115
https://doi.org/10.1139/o01-115
Publikováno v:
Journal of Molecular Biology. 309:975-988
The interactions that drive the folding of beta-barrel membrane proteins have not been well studied because there have been few available model systems for membrane beta-sheets. In this work, we expand on a recently described model system to explore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3569d78d8c1830f2de8bef0cfbbb7492
https://doi.org/10.1006/jmbi.2001.4715
https://doi.org/10.1006/jmbi.2001.4715
Publikováno v:
ResearcherID
The complex kinetic behavior commonly observed in protein folding studies suggests that a heterogeneous population of molecules exists in solution and that a number of discrete steps are involved in the conversion of unfolded molecules to the fully n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d095416ae22fadc13eeb31f8ffadf352
https://doi.org/10.1021/bi9700476
https://doi.org/10.1021/bi9700476
Publikováno v:
Antimicrobial agents and chemotherapy. 57(7)
We recently described a family of cationic antimicrobial peptides (CAMPs) selected from a combinatorial library that exhibited potent, broad-spectrum activity at neutral pH and low ionic strength. To further delimit the utility and activity profiles
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a74ea6e698b409264a4e6a87c700c98e
https://pubmed.ncbi.nlm.nih.gov/23650166
https://pubmed.ncbi.nlm.nih.gov/23650166
Autor:
Thomas C. Pinkerton, William M. Westler, Jun Haginaka, Eldon L. Ulrich, W. Jeffrey. Howe, Tokiko Murashima, Joseph P. Comiskey, John L. Markley, William F. Walkenhorst
Publikováno v:
Analytical Chemistry. 67:2354-2367
Individual protein domains and two domains in combination were prepared by enzymatic and chemical cleavage of turkey ovomucoid followed by isolation and purification by size-exclusion and ion-exchange chromatography. Silica bonded-phase HPLC columns
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::669fb31d0bec22a5c620bdb22b8583c7
https://doi.org/10.1021/ac00110a006
https://doi.org/10.1021/ac00110a006
Autor:
Stewart N. Loh, Dagmar M. Truckses, William F. Walkenhorst, Kenneth E. Prehoda, Jinfeng Wang, John L. Markley, Andrew P. Hinck
Publikováno v:
Pure and Applied Chemistry. 66:65-69
We have used NMR spectroscopy to determine peptide bond configurations and to measure the rates and equilibria of interconversion at individual Xaa-Pro peptide bond linkages in staphylococcal nuclease and several variants produced by site-directed mu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::297184e7469747f388740c5d7ac67139
https://doi.org/10.1351/pac199466010065
https://doi.org/10.1351/pac199466010065