Search Results - "Apiyo, David"

Role of cofactors in metalloprotein folding by Wilson, Corey J, Apiyo, David, Wittung-Stafshede, Pernilla

“…Metals are commonly found as natural constituents of proteins. Since many such metals can interact specifically with their corresponding unfolded proteins in…”
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Dissecting Homo-Heptamer Thermodynamics by Isothermal Titration Calorimetry: Entropy-Driven Assembly of Co-Chaperonin Protein 10 by Luke, Kathryn, Apiyo, David, Wittung-Stafshede, Pernilla

“…Normally, isothermal titration calorimetry (ITC) is used to study binding reactions between two different biomolecules. Self-association processes leading to…”
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Molecular basis of the structural stability of a Top7-based scaffold at extreme pH and temperature conditions by Soares, Thereza A., Boschek, Curt B., Apiyo, David, Baird, Cheryl, Straatsma, T.P.

“…The development of stable biomolecular scaffolds that can tolerate environmental extremes has considerable potential for industrial and defense-related…”
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Immobilization strategies for single-chain antibody microarrays by Seurynck-Servoss, Shannon L, Baird, Cheryl L, Miller, Keith D, Pefaur, Noah B, Gonzalez, Rachel M, Apiyo, David O, Engelmann, Heather E, Srivastava, Sudhir, Kagan, Jacob, Rodland, Karin D, Zangar, Richard C

“…Sandwich ELISA microarrays have great potential for validating disease biomarkers. Each ELISA relies on robust-affinity reagents that retain activity when…”
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Engineering an ultra-stable affinity reagent based on Top7 by Boschek, Curt B., Apiyo, David O., Soares, Thereza A., Engelmann, Heather E., Pefaur, Noah B., Straatsma, Tjerk P., Baird, Cheryl L.

“…Antibodies are widely used for diagnostic and therapeutic applications because of their sensitive and specific recognition of a wide range of targets; however,…”
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Unique complex between bacterial azurin and tumor-suppressor protein p53 by Apiyo, David, Wittung-Stafshede, Pernilla

“…The tumor-suppressor protein p53 is a major player in regulation of cell growth, genomic stability, and cell death. Recent work suggests that Pseudomonas…”
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Presence of the cofactor speeds up folding of Desulfovibrio desulfuricans flavodoxin by Apiyo, David, Wittung‐Stafshede, Pernilla

“…Flavodoxin is an α/β protein with a noncovalently bound flavin‐mononucleotide (FMN) cofactor. The apo‐protein adopts a structure identical to that of the…”
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Solvation of the folding‐transition state in Pseudomonas aeruginosa azurin is modulated by metal by Wilson, Corey J., Apiyo, David, Wittung‐Stafshede, Pernilla

“…The role of water in protein folding, specifically its presence or not in the transition‐state structure, is an unsolved question. There are two common classes…”
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Role of the Unique Peptide Tail in Hyperthermostable Aquifex aeolicus Cochaperonin Protein 10 by Luke, Kathryn, Apiyo, David, Wittung-Stafshede, Pernilla

“…All known cochaperonin protein 10 (cpn10) molecules are heptamers of seven identical subunits noncovalently linked by β-strand interactions. Cpn10 from the…”
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X-ray Structure of the R69D Phosphatidylinositol-Specific Phospholipase C Enzyme:  Insight into the Role of Calcium and Surrounding Amino Acids in Active Site Geometry and Catalysis by Apiyo, David, Zhao, Li, Tsai, Ming-Daw, Selby, Thomas L

“…Phosphatidylinositol-specific phospholipase Cs (PLCs) are a family of phosphodiesterases that catalyze the cleavage of the P−O bond via transesterification…”
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Solvation of the folding-transition state in Pseudomonas aeruginosa azurin is modulated by metal: Solvation of azurin's folding nucleus by Wilson, Corey J, Apiyo, David, Wittung-Stafshede, Pernilla

“…The role of water in protein folding, specifically its presence or not in the transition-state structure, is an unsolved question. There are two common classes…”
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Equilibrium Unfolding of Dimeric Desulfoferrodoxin Involves a Monomeric Intermediate:  Iron Cofactors Dissociate after Polypeptide Unfolding by Apiyo, David, Jones, Kathryn, Guidry, Jesse, Wittung-Stafshede, Pernilla

“…Here we report the conformational stability of homodimeric desulfoferrodoxin (dfx) from Desulfovibrio desulfuricans (ATCC 27774). The dimer is formed by two…”
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The role of the cofactors in folding of Desulfovibrio desulfuricans flavodoxin and desulfoferrodoxin (DFX) by Apiyo, David Odanga

“…In this thesis, the roles of the cofactors for folding and stability of flavodoxin and desulfoferredoxin proteins from Desulfovibrio desulfuricans , a…”
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The role of the cofactors in folding of Desulfovibrio desulfuricans flavodoxin and desulfoferrodoxin (DFX) by Apiyo, David Odanga

“…In this thesis, the roles of the cofactors for folding and stability of flavodoxin and desulfoferredoxin proteins from Desulfovibrio desulfuricans , a…”
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No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin by Apiyo, David, Guidry, Jesse, Wittung-Stafshede, Pernilla

“…Flavodoxins are proteins with an α/β doubly wound topology that mediate electron transfer through a non-covalently bound flavin mononucleotide (FMN). The FMN…”
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