Search Results - "Sood, Satish M."

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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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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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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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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Association of mixtures of the two major forms of beta-casein from human milk by Sood, S M, Slattery, C W

“…Human milk beta-casein (CN) is unique in that it may be phosphorylated at any level from zero (beta-CN-0P) to five (beta-CN-5P) organic phosphates per…”
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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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Thermal Cycling Aids Folding of a Recombinant Human β-Casein with Four Extra N-Terminal Amino Acid Residues by Hu, YiLin, Sood, Satish M., Slattery, Charles W.

“…Due to the limited secondary structure, it is believed that the caseins of milk, particularly the β-caseins (β-CN), may be in a mostly random-coil conformation…”
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Monomer characterization and studies of self-association of the major beta-casein of human milk by Sood, S M, Slattery, C W

“…The casein form that has four organic phosphoryl groups, beta-casein (CN)-4P, is the major constituent (approximately 35%) of the beta-CN fraction of human…”
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Structural studies on casein micelles of human milk: dissociation of beta-casein of different phosphorylation levels induced by cooling and ethylenediaminetetraacetate by Sood, S M, Herbert, P J, Slattery, C W

“…Information on the structure of human casein micelles has been obtained from dissociation of beta-casein (CN). Two approaches were used: cooling at 4 degrees C…”
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Characterization of Zinc-Depleted Alanyl-tRNA Synthetase from Escherichia coli: Role of Zinc by Sood, Satish M., Wu, Min-Xian, Hill, Kelvin A.W., Slattery, Charles W.

“…To evaluate the role of zinc in Escherichia coli alanyl-tRNA synthetase, hydrodynamic measurements and circular dichroism spectra were obtained for the…”
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The pH-dependent dissociation of beta-casein from human milk micelles: role of electrostatic interactions by Sood, S M, Herbert, P J, Slattery, C W

“…Evidence has been reported that supports the role of hydrophobic interactions in the association of the monomers and in the dissociation of different…”
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