Zobrazeno 1 - 10
of 13
pro vyhledávání: '"William 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
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
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
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
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
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
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
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
Publikováno v:
"Protein Engineering, Design and Selection". 6:221-227
Genetic engineering studies of ovomucoid domains have been hindered by the lack of an efficient procedure for overproducing this protein. The novel scheme presented here has led to the isolation of chicken ovomucoid third domain (OMCHI3) at a level o
Publikováno v:
Biochemistry. 31:911-920
The backbone 1H and 15N resonances of unligated staphylococcal nuclease H124L (recombinant protein produced in Escherichia coli whose sequence is identical to the nuclease produced by the V8 strain of Staphylococcus aureus) have been assigned by thre