Výsledky vyhledávání - "Pamela J. Low"

Active Sites in Complement Components C5 and C3 Identified by Proximity to Indels in the C3/4/5 Protein Family

Autor: Pamela J. Low, Rong Ai, Ronald T. Ogata

Publikováno v: The Journal of Immunology. 162:6580-6588

We recently suggested that sites of length polymorphisms in protein families (indels) might serve as useful guides for locating protein:protein interaction sites. This report describes additional site-specific mutagenesis and synthetic peptide inhibi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fd9f403af8f01c91fa80e486ab24d951
https://doi.org/10.4049/jimmunol.162.11.6580

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Active Sites in Complement Component C3 Mapped by Mutations at Indels

Autor: Ronald T. Ogata, Rong Ai, Pamela J. Low

Publikováno v: The Journal of Immunology. 161:4785-4794

Engineered mutants of human complement component C3 were used to test the idea that sites of length polymorphisms in protein families (indels) can guide a search for protein:protein interaction sites. Sequence changes were introduced at each of the 2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::492856ca1800a443db585a29a2c1cf1d
https://doi.org/10.4049/jimmunol.161.9.4785

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Thermodynamics of Fatty Acid Binding to Engineered Mutants of the Adipocyte and Intestinal Fatty Acid-binding Proteins

Autor: Pamela J. Low, Alan M. Kleinfeld, Gary V. Richieri, Ronald T. Ogata

Publikováno v: Journal of Biological Chemistry. 273:7397-7405

We constructed 18 single amino acid mutants of the adipocyte fatty acid-binding protein (A-FABP) and 17 of the intestinal fatty acid-binding protein (I-FABP), at locations in the fatty acid (FA) binding sites. For each mutant protein, we measured the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d3787af6c49831947d0b9a949d808fb
https://doi.org/10.1074/jbc.273.13.7397

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Binding kinetics of engineered mutants provide insight about the pathway for entering and exiting the intestinal fatty acid binding protein

Autor: Ronald T. Ogata, Pamela J. Low, Gary V. Richieri, Alan M. Kleinfeld

Publikováno v: Biochemistry. 38(18)

To better understand the mechanism by which fatty acids bind to and dissociate from the binding cavities of fatty acid binding proteins (FABPs), we constructed 31 single amino acid mutants of the intestinal FABP (I-FABP) and determined the rate const

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a5cec6d4c25ad09ea0b7010bd922c36
https://pubmed.ncbi.nlm.nih.gov/10231541

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Mutants of rat intestinal fatty acid-binding protein illustrate the critical role played by enthalpy-entropy compensation in ligand binding

Autor: Gary V. Richieri, Alan M. Kleinfeld, Pamela J. Low, Ronald T. Ogata

Publikováno v: The Journal of biological chemistry. 272(27)

Site-specific variants of rat intestinal fatty acid-binding protein were constructed to identify the molecular interactions that are important for binding to fatty acids (FAs). Several variants displayed affinities that appeared incompatible with the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3748207983d494a5c43ce0f8df7f7c5
https://pubmed.ncbi.nlm.nih.gov/9201976

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