Search Results - "Seale, Jeffrey W."

Structure of the full‐length insecticidal protein Cry1Ac reveals intriguing details of toxin packaging into in vivo formed crystals by Evdokimov, Artem G., Moshiri, Farhad, Sturman, Eric J., Rydel, Timothy J., Zheng, Meiying, Seale, Jeffrey W., Franklin, Sonya

“…For almost half a century, the structure of the full‐length Bacillus thuringiensis (Bt) insecticidal protein Cry1Ac has eluded researchers, since Bt‐derived…”
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The role of a conserved histidine-tyrosine interhelical interaction in the ion channel domain of δ-endotoxins from Bacillus thuringiensis by Seale, Jeffrey W.

“…The δ‐endotoxin proteins are produced by Bacillus thuringiensis during the sporulation phase of its life cycle. These proteins exhibit insecticidal activity…”
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Climate smart agriculture opportunities for mitigating soil greenhouse gas emissions across the U.S. Corn-Belt by McNunn, Gabriel, Karlen, Douglas L., Salas, William, Rice, Charles W., Mueller, Steffen, Muth, David, Seale, Jeffrey W.

“…Widespread adoption of climate smart agriculture (CSA) has the potential to greatly mitigate agricultural greenhouse gas (GHG) emissions by increasing soil…”
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Photoincorporation of 4,4'-Bis(1-anilino-8-naphthalenesulfonic Acid) into the Apical Domain of GroEL: Specific Information from a Nonspecific Probe by Seale, Jeffrey W, Martinez, Jennifer L, Horowitz, Paul M

“…The use of noncovalent hydrophobic probes such as bis-ANS has become increasingly popular in gaining structural information about protein structure and…”
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Residual Structure in Urea-Denatured Chaperonin GroEL by Gorovits, Boris M, Seale, Jeffrey W, Horowitz, Paul M

“…The urea denaturation of the chaperonin GroEL has been studied by circular dichroism, intrinsic tyrosine fluorescence and fluorescence of the hydrophobic…”
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The C-terminal Sequence of the Chaperonin GroES Is Required for Oligomerization (∗) by Seale, Jeffrey W., Horowitz, Paul M.

“…The Escherichia coli protein GroES is a co-chaperonin that is able to assist GroEL in the refolding of proteins. GroES is a heptamer of seven identical…”
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Conditions for Nucleotide-dependent GroES-GroEL Interactions by Gorovits, Boris M., Ybarra, Jesse, Seale, Jeffrey W., Horowitz, Paul M.

“…A still unresolved question regarding the mechanism of chaperonin-assisted protein folding involves the stoichiometry of the GroEL-GroES complex. This is…”
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Structure of the full‐length insecticidal protein C ry1 A c reveals intriguing details of toxin packaging into in vivo formed crystals by Evdokimov, Artem G., Moshiri, Farhad, Sturman, Eric J., Rydel, Timothy J., Zheng, Meiying, Seale, Jeffrey W., Franklin, Sonya

“…For almost half a century, the structure of the full‐length Bacillus thuringiensis ( Bt ) insecticidal protein Cry1Ac has eluded researchers, since Bt ‐derived…”
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The role of a conserved histidine-tyrosine interhelical interaction in the ion channel domain of [delta]-endotoxins from Bacillus thuringiensis by Seale, Jeffrey W

“…The [delta]-endotoxin proteins are produced by Bacillus thuringiensis during the sporulation phase of its life cycle. These proteins exhibit insecticidal…”
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Preformed GroES oligomers are not required as functional cochaperonins by Seale, J W, Chirgwin, J M, Demeler, B, Horowitz, P M

“…We have previously shown that the C-terminal sequence of GroES is required for oligomerization [Seale and Horowitz (1995), J. Biol. Chem. 270, 30268-30270]. In…”
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Sequence determinants of the capping box, a stabilizing motif at the N‐termini of α‐helices by Seale, Jeffrey W., Srinivasan, Rajgopal, Rose, George D.

“…The capping box, a recurrent hydrogen bonded motif at the N‐termini of α‐helices, caps 2 of the initial 4 backbone amide hydrogen donors of the helix (Harper…”
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Reversible Oligomerization and Denaturation of the Chaperonin GroES by Seale, Jeffrey W., Gorovits, Boris M., Ybarra, Jesse, Horowitz, Paul M.

“…The chaperonin GroEL can assist protein folding and normally acts with the co-chaperonin GroES. These Escherichia coli proteins are encoded on the same operon,…”
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Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides by Gorovits, B M, Ybarra, J, Seale, J W, Horowitz, P M

“…A still unresolved question regarding the mechanism of chaperonin-assisted protein folding involves the stoichiometry of the GroEL-GroES complex. This is…”
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Photoincorporation of fluorescent probe into GroEL: defining site of interaction by Seale, J W, Brazil, B T, Horowitz, P M

“…We have elucidated conditions for the covalent incorporation of a nonspecific hydrophobic probe, bisANS, into various proteins. Using this method, we are able…”
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