Search Results - "Brems, D N"

Secondary structure of amyloid beta peptide correlates with neurotoxic activity in vitro by Simmons, L K, May, P C, Tomaselli, K J, Rydel, R E, Fuson, K S, Brigham, E F, Wright, S, Lieberburg, I, Becker, G W, Brems, D N

“…Amyloid beta peptide (A beta), the major protein constituent of senile plaques in patients with Alzheimer's disease, is believed to facilitate the progressive…”
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Characterization and stability of N-terminally PEGylated rhG-CSF by KINSTLER, O. B, BREMS, D. N, LAUREN, S. L, PAIGE, A. G, HAMBURGER, J. B, TREUHEIT, M. J

“…The liquid stability of rhG-CSF was investigated after polyethylene glycol (PEG) with an average molecular weight of 6000 daltons was covalently attached to…”
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The effects of alpha-helix on the stability of Asn residues: Deamidation rates in peptides of varying helicity by KOSKY, ANDREW A., RAZZAQ, URSULA O., TREUHEIT, MICHAEL J., BREMS, DAVID N.

“…Asn deamidation was monitored in Ala-based octadecapeptides of varying α-helicity. Gly was substituted for Ala residues at positions 6 and 16 to create a…”
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Nature of the Charged-Group Effect on the Stability of the C-Peptide Helix by Shoemaker, Kevin R., Kim, Peter S., Brems, David N., Marqusee, Susan, York, Eunice J., Chaiken, Irwin M., Stewart, John M., Baldwin, Robert L.

“…The residues responsible for the pH-dependent stability of the helix formed by the isolated C-peptide (residues 1-13 of ribonuclease A) have been identified by…”
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Altering the association properties of insulin by amino acid replacement by Brems, D N, Alter, L A, Beckage, M J, Chance, R E, DiMarchi, R D, Green, L K, Long, H B, Pekar, A H, Shields, J E, Frank, B H

“…The importance of ProB28 and LysB29 on the self-association of insulin was established by systematically truncating the C terminus of the B chain. The…”
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Solubility of different folding conformers of bovine growth hormone by Brems, David N.

“…Previous folding studies have shown that equilibrium denaturation of bovine growth hormone (bGH) is a multistate process with stable intermediates. The native…”
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Specific interaction between beta-lactams and soluble penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus: development of a chromogenic assay by ROYCHOUDHURY, S, KAISER, R. E, BREMS, D. N, YEH, W.-K

“…Services AAC Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon…”
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Equilibrium denaturation of human growth hormone and its cysteine-modified forms by BREMS, D. N, BROWN, P. L, BECKER, G. W

“…The equilibrium denaturation of human growth hormone (hGH) derived from heterologous gene expression in Escherichia coli was studied. Denaturation was measured…”
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PEGylation prevents the N-terminal degradation of Megakaryocyte Growth and Development Factor by GUERRA, P. I, ACKLIN, C, KOSKY, A. A, DAVIS, J. M, TREUHEIT, M. J, BREMS, D. N

“…Determine the effect of PEGylation on in-vitro degradation for recombinant human Megakaryocyte Growth and Development Factor (rHuMGDF) in the neutral pH range…”
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Manipulation of the observed kinetic phases in the refolding of denatured ferricytochromes c by Brems, D N, Stellwagen, E

“…The refolding of guanidine hydrochloride-denatured horse heart ferricytochrome c at pH 7.0 and 23 degrees C occurs in three kinetic phases as observed by…”
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Evidence for a self-associating equilibrium intermediate during folding of human growth hormone by DeFelippis, Michael R, Alter, Leila A, Pekar, Allen H, Havel, Henry A, Brems, David N

“…It has been previously shown, by equilibrium denaturation, that human growth hormone (hGH) folds by a cooperative two-state process. This is in contrast to the…”
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Stabilization of an Associated Folding Intermediate of Bovine Growth Hormone by Site-Directed Mutagenesis by Brems, David N., Plaisted, Scott M., Havel, Henry A., Tomich, Che-Shen C.

“…By using oligonucleotide-directed mutagenesis, Lys-112 of bovine growth hormone (bGH) was changed to leucine, and its resulting effect on folding was studied…”
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Characterization of an associated equilibrium folding intermediate of bovine growth hormone by Brems, D. N, Plaisted, S. M, Kauffman, E. W, Havel, H. A

“…In the preceding paper [Havel, H. A., Kauffman, E. W., Plaisted, S. M., & Brems, D. N. (1986) Biochemistry (preceding paper in this issue)], an associated…”
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Acid stabilization of insulin by Bryant, Christopher, Spencer, Donald B, Miller, Alita, Bakaysa, Diane L, McCune, Karen S, Maple, Steven R, Pekar, Allen H, Brems, David N

“…The effect of pH on the conformational stability of insulin was studied. Surprisingly, the Gibbs free energy of unfolding increased approximately 30% by…”
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Reversible self-association of bovine growth hormone during equilibrium unfolding by Havel, H. A, Kauffman, E. W, Plaisted, S. M, Brems, D. N

“…Previous investigations have shown that bovine growth hormone (bGH, somatotropin) unfolds through a reversible multistate process with at least one stable…”
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Equilibrium denaturation of insulin and proinsulin by Brems, David N, Brown, Patricia L, Heckenlaible, Leila A, Frank, Bruce H

“…The guanidine hydrochloride induced equilibrium denaturation of insulin and proinsulin was studied by using near- and far-ultraviolet (UV) circular dichroism…”
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Folding of bovine growth hormone is consistent with the molten globule hypothesis by Brems, D N, Havel, H A

“…Previous results from equilibrium and kinetic studies of the folding of bovine growth hormone (bGH) have demonstrated that bGH does not follow a simple…”
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The kinetics of bovine growth hormone folding are consistent with a framework model by Brems, D.N., Plaisted, S.M., Dougherty, J.J., Holzman, T.F.

“…The framework model of protein folding requires the hydrogen-bonded secondary structure to be formed early in folding (i.e. the formation of secondary…”
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The conformational stability and flexibility of insulin with an additional intramolecular cross-link by BREMS, D. N, BROWN, P. L, NAKAGAWA, S. H, TAGER, H. S

“…The conformational stability and flexibility of insulin containing a cross-link between the alpha-amino group of the A-chain to the epsilon-amino group of…”
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Refolding and purification of Cephalosporium acremonium deacetoxycephalosporin C synthetase/hydroxylase from granules of recombinant Escherichia coli by Ghag, S K, Brems, D N, Hassell, T C, Yeh, W K

“…The gene for bifunctional deacetoxycephalosporin C synthetase/hydroxylase of Cephalosporium acremonium was cloned and overexpressed as an insoluble and…”
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