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Protein synthesis - wonderwhizkids

This review summarizes the progress in the synthesis of close models of complex metalloproteins, followed by a description of recent advances in using the approach for making novel compounds that are unprecedented in either inorganic chemistry or biology.

(rather than the deceleration of protein synthesis) ..

The two independent Cu-Cu distances of 2.42 and 2.35 Å (with respective concomitant adjustments of ligand-Cu distances) are consistent with that (2.39 Å) obtained from X-ray absorption spectroscopy with the same molecule, and are among the shortest Cu-Cu bonds observed to date in proteins or inorganic complexes.

Protein Synthesis and Degradation | Basicmedical Key

Currently, all three approaches are being used effectively in elucidating the structure and function of naturally occurring metalloproteins.

Laser excitation of the Zn-porphyrin (ZnP) to its triplet excited state (3ZnP) initiates direct heme-heme ET to the ferriheme center of its partner across the protein-protein interface.

This difference may translate into a much wider range of reduction potentials (>1000 mV) for blue copper proteins that transfer electrons to a variety of partners in many different biological systems and a much narrower range of reduction potentials (

Chapter 13 Protein Synthesis and ..

UV−vis studies of the resting state of the designed protein swMb((L29H, F43H) (called CuBMb) suggest that a single copper-binding site is created in swMb.

Organic chemistry: “Amino acid and polypeptide synthesis”. Amino acid synthesis--Gabriel synthesis; synthesis. degradation. Polypeptide synthesis-- () and () amino-protecting groups; protection of the terminus via ester formation; DCC () -activating reagent. An example of calculating and charge at a specific pH for a long polypeptide

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A Bilirubin-Inducible Fluorescent Protein from Eel …

In the process, it introduces the CuA center in four different systems---native protein systems, soluble protein truncates of native proteins, synthetic models using organic molecules, and biosynthetic models using proteins as ligands---with a greater emphasis on biosynthetic models of CuA, especially on new, deeper insights gained from their studies.

Dystrophin-Glycoprotein Complexes

Here, we review the contribution of protein engineering approaches, namely, the incorporation of unnatural amino acids and a biosynthetic CuA cofactor into the T1 copper protein azurin, to advancing the current understanding of how the unique structures of T1 copper and CuA centers confer their proteins with efficient and tailored ET properties.

Chemistry Courses » Chemistry | Boston University

Replication of DNA plays a central role in transmitting hereditary information from cell to cell. To achieve reliable DNA replication, multiple proteins form a stable complex, known as the replisome, enabling them to act together in a highly coordinated fashion. Over the past decade, the roles of the various proteins within the replisome have been determined. Although many of their interactions have been characterized, it remains poorly understood how replication proteins enter and leave the replisome. In this study, we visualize fluorescently labeled bacteriophage T7 DNA polymerases within the replisome while we simultaneously observe the kinetics of the replication process. This combination of observables allows us to monitor both the activity and dynamics of individual polymerases during coordinated leading-and lagging-strand synthesis. Our data suggest that lagging-strand polymerases are exchanged at a frequency similar to that of Okazaki fragment synthesis and that two or more polymerases are present in the replisome during DNA replication. Our studies imply a highly dynamic picture of the replisome with lagging-strand DNA polymerases residing at the fork for the synthesis of only a few Okazaki fragments. Further, new lagging-strand polymerases are readily recruited from a pool of polymerases that are proximally bound to the replisome and continuously replenished from solution.

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Although the redesign of existing metal-binding sites in naturally occurring proteins still offers the most promise for a successful design, the more challenging goal of engineering metal-binding sites in de novo designed proteins and peptides is being achieved with increasing frequency.

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