Search Results - "Slattery, Charles W."

A folding pattern that is stable to thermal cycling is achieved by long term storage of recombinant human beta-casein with four extra N-terminals amino-acid residues at -20 degrees C by Sood, Satish M, Booth, Cassie, Jhawar, Harbir, Slattery, Charles W

“…Studies have followed the turbidity (OD400 nm) of beta-casein (CN) as temperature (T) increased from 4 to 37 degrees C. Native non-phosphorylated beta-CN…”
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The effect of conserved residue charge reversal on the folding of recombinant non-phosphorylated human β-casein by Bu, Hongyin, Sood, Satish M, Slattery, Charles W

“…A short stretch of 13 amino acids in the central portion of human β-casein contains four positively charged conserved residues, three Lys and one Arg. We…”
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Comparison of native and recombinant non-phosphorylated human β-casein: further evidence for a unique β-casein folding pattern by Bu, Hongyin, Hu, Yilin, Sood, Satish M, Slattery, Charles W

“…Recombinant wild-type non-phosphorylated human β-casein was obtained from Escherichia coli. Turbidity vs. temperature (T) without Ca 2+ showed wild-type…”
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Reconstituted micelle formation using reduced, carboxymethylated bovine kappa-casein and human beta-casein by Sood, Satish M, Lekic, Tim, Jhawar, Harbir, Farrell, Jr, Harold M, Slattery, Charles W

“…In milk, kappa-casein, a mixture of disulfide-bonded polymers, stabilizes and regulates the size of the unique colloidal complex of protein, Ca2+ and inorganic…”
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The Effect of C-Terminal Deletion on the Folding and Self-association of Recombinant Non-phosphorylated Human ß-Casein by Bu, Hongyin, Sood, Satish M., Slattery, Charles W.

“…Recombinant human ß-casein (CN) mutants were prepared having 11, 22 and 31 amino acids (aa) deleted from the C-terminus. The temperature-dependent…”
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Colloidal calcium phosphate in the reconstituted milk micelle may direct wild-type recombinant human beta-casein to fold like the native protein by Sood, Satish M, Erickson, Grant, Jhawar, Harbor, Slattery, Charles W

“…Native human beta-casein (CN) at all phosphorylation levels exhibits reproducible behavior and appears to have a unique, stable folding pattern. In contrast,…”
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The formation of casein micelles reconstituted with Ca+2 and added inorganic phosphate is influenced by the non-phosphorylated form of human beta-casein by Sood, Satish M, Erickson, Grant, Slattery, Charles W

“…The beta-casein (CN) human milk fraction is comprised of a single protein phosphorylated at levels from 0 to 5. Component interactions are dependent on the…”
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The effect of C-terminal deletion on the folding and self-association of recombinant non-phosphorylated human beta-casein by Bu, Hongyin, Sood, Satish M, Slattery, Charles W

“…Recombinant human beta-casein (CN) mutants were prepared having 11, 22 and 31 amino acids (aa) deleted from the C-terminus. The temperature-dependent…”
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Review: Casein micelle structure; an examination of models by Slattery, C W

“…The casein micelle system of bovine milk is unique in that protein aggregates of similar spherical shape but extreme variability of size are formed by the…”
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Evaluation of PCR-ELISA for determination of telomerase activity in prostate needle biopsy and prostatic fluid specimens by Wang, Zhilian, Ramin, Soroush A., Tsai, Christopher, Lui, Paul, Ruckle, Herbert C., Beltz, Richard E., Sands, John F., Slattery, Charles W.

“…The conventional TRAP assay will determine telomerase activity in tissue or other specimens. However, methodological disadvantages limit its clinical use. We…”
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Binding of cations to caseins. Site binding, Donnan binding, and system characteristics by Waugh, David F, Slattery, Charles W, Creamer, Lawrence K

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A folding pattern that is stable to thermal cycling is achieved by long term storage of recombinant human β-casein with four extra N-terminals amino-acid residues at −20 °C by Sood, Satish M., Booth, Cassie, Jhawar, Harbir, Slattery, Charles W.

“…Studies have followed the turbidity (OD 400 nm) of β-casein (CN) as temperature ( T) increased from 4 to 37 °C. Native non-phosphorylated β-CN showed a…”
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Variation in the glycosylation pattern of bovine κ-casein with micelle size and its relationship to a micelle model by Slattery, Charles W

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Interactions of doubly phosphorylated human β‐casein with native and reduced, carboxymethylated bovine κ‐casein leading to micelle formation: Role of inorganic phosphate by Sood, Satish M, Booth, Cassie, Jhawar, Harbir S, Farrell, Harold M, Slattery, Charles W

“…Milk micelles are largely colloidal complexes of casein (CN) phosphoproteins. The reconstituted micelle system in the absence of inorganic phosphate (Pi) is…”
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Colloidal Calcium Phosphate in the Reconstituted Milk Micelle May Direct Wild-type Recombinant Human [beta]-Casein to Fold Like the Native Protein by Sood, Satish M, Erickson, Grant, Jhawar, Harbor, Slattery, Charles W

“…Native human β-casein (CN) at all phosphorylation levels exhibits reproducible behavior and appears to have a unique, stable folding pattern. In contrast, the…”
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The Formation of Casein Micelles Reconstituted with Ca+2 and Added Inorganic Phosphate is Influenced by the Non-phosphorylated Form of Human [beta]-Casein by Sood, Satish M, Erickson, Grant, Slattery, Charles W

“…The β-casein (CN) human milk fraction is comprised of a single protein phosphorylated at levels from 0 to 5. Component interactions are dependent on the…”
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A model for the formation and structure of casein micelles from subunits of variable composition by Slattery, C W, Evard, R

“…Sedimentation coefficients were determined for association products in systems containing SH-kappa-casein, SH-kappa-casein-alpha(S1) or beta-caseins (1:1, by…”
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Reconstituted Micelle Formation Using Reduced, Carboxymethylated Bovine [kappa]-Casein and Human [beta]-Casein by Sood, Satish M, Lekic, Tim, Jhawar, Harbir, Farrell, Harold M, Slattery, Charles W

“…In milk, κ-casein, a mixture of disulfide-bonded polymers, stabilizes and regulates the size of the unique colloidal complex of protein, Ca^sup 2+^ and…”
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Core polymers of casein micelles by Waugh, David F, Creamer, Lawrence K, Slattery, Charles W, Dresdner, George W

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Stability ofEscherichia coliAlanyl-tRNA Synthetase Quaternary Structure under Increased Pressure by Sood, Satish M., Hill, Kelvin A.W., Slattery, Charles W.

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