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Articles 1 - 4 of 4
Full-Text Articles in Social and Behavioral Sciences
Site-Specific Covalent Attachment Of Dna To Proteins Using A Photoactivatable Tus-Ter Complex, Dahdah B. Dahdah, Isabelle Morin, Morgane Moreau, Nicholas E. Dixon, Patrick M. Schaeffer
Site-Specific Covalent Attachment Of Dna To Proteins Using A Photoactivatable Tus-Ter Complex, Dahdah B. Dahdah, Isabelle Morin, Morgane Moreau, Nicholas E. Dixon, Patrick M. Schaeffer
Faculty of Science - Papers (Archive)
Investigations into the photocrosslinking kinetics of the protein Tus with various bromodeoxyuridine-substituted Ter DNA variants highlight the potential use of this complex as a photoactivatable connector between proteins of interest and specific DNA sequences.
Glutarate And N-Acetyl-L-Glutamate Buffers For Cell-Free Synthesis Of Selectively 15n-Labelled Proteins, X Jia, Kiyoshi Ozawa, K Loscha, G Otting
Glutarate And N-Acetyl-L-Glutamate Buffers For Cell-Free Synthesis Of Selectively 15n-Labelled Proteins, X Jia, Kiyoshi Ozawa, K Loscha, G Otting
Faculty of Science - Papers (Archive)
Cell-free protein synthesis provides rapid and economical access to selectively 15N-labelled proteins, greatly facilitating the assignment of 15N-HSQC spectra. While the best yields are usually obtained with buffers containing high concentrations of potassium L-glutamate, preparation of selectively 15N-Glu labelled samples requires non-standard conditions. Among many compounds tested to replace the L-Glu buffer, potassium N-acetyl-L-glutamate and potassium glutarate were found to perform best, delivering high yields for all proteins tested, with preserved selectivity of 15N-Glu labelling. Assessment of amino-transferase activity by combinatorial 15N-labelling revealed that glutarate and N-acetyl-L-glutamate suppress the transfer of the 15N-alpha-amino groups between amino acids less well than …
Crystallin Proteins And Amyloid Fibrils, Heath Ecroyd, John A. Carver
Crystallin Proteins And Amyloid Fibrils, Heath Ecroyd, John A. Carver
Faculty of Science - Papers (Archive)
Improper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates. The major lens protein, alpha-crystallin, is a member of the small heat-shock protein (sHsp) family of intracellular molecular chaperone proteins that prevent protein aggregation. Whilst the chaperone activity of sHsps against amorphously aggregating proteins has been well studied, its action against fibril-forming proteins has received less attention despite the presence of sHsps in deposits found in fibril-associated diseases (e.g. Alzheimer's and Parkinson's). In this review, the literature on the interaction of alpha B-crystallin and other sHsps with fibril-forming proteins is summarized. In particular, …
New Proteins Identified In Epididymal Fluid From The Platypus (Ornithorhynchus Anatinus), Jean-Louis Dacheux, Francoise Dacheux, Valerie Labas, Heath Ecroyd, Brett Nixon, Russell C. Jones
New Proteins Identified In Epididymal Fluid From The Platypus (Ornithorhynchus Anatinus), Jean-Louis Dacheux, Francoise Dacheux, Valerie Labas, Heath Ecroyd, Brett Nixon, Russell C. Jones
Faculty of Science - Papers (Archive)
The platypus epididymal proteome is being studied because epididymal proteins are essential for male fertility in mammals and it is considered that knowledge of the epididymal proteome in an early mammal would be informative in assessing the convergence and divergence of proteins that are important in the function of the mammalian epididymis. Few of the epididymal proteins that have been identified in eutherian mammals were found in platypus caudal epididymal fluid, and the major epididymal proteins in the platypus (PXN-FBPL, SPARC and E-OR20) have never been identified in the epididymis of any other mammal.