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Srinivasan Muniyappan

Researcher at Daegu Gyeongbuk Institute of Science and Technology

Publications -  19
Citations -  238

Srinivasan Muniyappan is an academic researcher from Daegu Gyeongbuk Institute of Science and Technology. The author has contributed to research in topics: Deubiquitinating enzyme & Chemistry. The author has an hindex of 6, co-authored 15 publications receiving 149 citations. Previous affiliations of Srinivasan Muniyappan include KAIST.

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Direct Observation of Cooperative Protein Structural Dynamics of Homodimeric Hemoglobin from 100 ps to 10 ms with Pump–Probe X-ray Solution Scattering

TL;DR: This work employed picosecond X-ray solution scattering and novel structural analysis to track the details of the structural dynamics of wild-type homodimeric hemoglobin from the clam Scapharca inaequivalvis and its F97Y mutant over a wide time range from 100 ps to 56.2 ms, providing new insights into the protein structural dynamics.
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Cooperative protein structural dynamics of homodimeric hemoglobin linked to water cluster at subunit interface revealed by time-resolved X-ray solution scattering.

TL;DR: Comparing the structures of protein intermediates in wild-type HbI and the T72V mutant, it is revealed how the perturbation in the interfacial water cluster affects the kinetics and structures of reaction intermediates of Hbi.
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Deubiquitination Reactions on the Proteasome for Proteasome Versatility.

TL;DR: The biology of proteasome-associated deubiquitination should be further elucidated for its potential targeting in human diseases.
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SVD-aided pseudo principal-component analysis: A new method to speed up and improve determination of the optimum kinetic model from time-resolved data.

TL;DR: The results of SAPPA for both time-resolved X-ray solution scattering (TRXSS) and transient absorption (TA) data of the same protein reveal that global structural changes of protein may occur more slowly than local structural changes around the chromophore, which is probed by TA spectroscopy.
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Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering

TL;DR: In this paper, femtosecond time-resolved X-ray solution scattering (fs-TRXSS) and a structure refinement method were applied to visualize the ultrafast motion of a protein.