Publications by authors named "Salman Tahir"

Article Synopsis
  • - QCLMS is a method that analyzes protein structure and dynamics by comparing the amounts of cross-links formed under different conditions, which helps reveal important changes in protein configuration.
  • - The study applied QCLMS to the human complement protein C3 and its derivative C3b, noting how small and large conformational changes influenced the detectability of protein cross-links.
  • - The researchers established a standardized workflow and coding practices to support QCLMS, positioning it as a valuable technique for tracking how proteins interact and change shape in various biological processes.
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Background: The zygoma plays an important role in the facial contour for both cosmetic and functional reasons; therefore zygomatic bone injuries should be properly diagnosed and adequately treated. Comparison of various surgical approaches and their complications can only be done objectively using outcome measurements which in turn require protocol management and long-term follow up. The preference for open reduction and internal fixation of zygomatic fractures at three points has continued to grow in response to observations of inadequate results from two point and one point fixation techniques.

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Higher-order multi-protein complexes such as RNA polymerase II (Pol II) complexes with transcription initiation factors are often not amenable to X-ray structure determination. Here, we show that protein cross-linking coupled to mass spectrometry (MS) has now sufficiently advanced as a tool to extend the Pol II structure to a 15-subunit, 670 kDa complex of Pol II with the initiation factor TFIIF at peptide resolution. The N-terminal regions of TFIIF subunits Tfg1 and Tfg2 form a dimerization domain that binds the Pol II lobe on the Rpb2 side of the active centre cleft near downstream DNA.

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