Adilakshmi Dwarasala - Academia.edu (original) (raw)

Adilakshmi Dwarasala

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Papers by Adilakshmi Dwarasala

Research paper thumbnail of ssPINE/ssPINE-POKY: Automated chemical shift assignment with an intuitive graphical user interface for solid-state NMR data from complex protein systems

Biophysical Journal, Feb 1, 2023

Research paper thumbnail of The POKY suite: The revolutionized platform for biomolecular studies

Biophysical Journal, Feb 1, 2023

Research paper thumbnail of ssPINE/ssPINE-POKY: Automated chemical shift assignment with an intuitive graphical user interface for solid-state NMR data from complex protein systems

Research paper thumbnail of The POKY suite: The revolutionized platform for biomolecular studies

Research paper thumbnail of ssPINE: Probabilistic Algorithm for Automated Chemical Shift Assignment of Solid-State NMR Data from Complex Protein Systems

Membranes

The heightened dipolar interactions in solids render solid-state NMR (ssNMR) spectra more difficu... more The heightened dipolar interactions in solids render solid-state NMR (ssNMR) spectra more difficult to interpret than solution NMR spectra. On the other hand, ssNMR does not suffer from severe molecular weight limitations like solution NMR. In recent years, ssNMR has undergone rapid technological developments that have enabled structure–function studies of increasingly larger biomolecules, including membrane proteins. Current methodology includes stable isotope labeling schemes, non-uniform sampling with spectral reconstruction, faster magic angle spinning, and innovative pulse sequences that capture different types of interactions among spins. However, computational tools for the analysis of complex ssNMR data from membrane proteins and other challenging protein systems have lagged behind those for solution NMR. Before a structure can be determined, thousands of signals from individual types of multidimensional ssNMR spectra of samples, which may have differing isotopic composition...

Research paper thumbnail of ssPINE/ssPINE-POKY: Automated chemical shift assignment with an intuitive graphical user interface for solid-state NMR data from complex protein systems

Biophysical Journal, Feb 1, 2023

Research paper thumbnail of The POKY suite: The revolutionized platform for biomolecular studies

Biophysical Journal, Feb 1, 2023

Research paper thumbnail of ssPINE/ssPINE-POKY: Automated chemical shift assignment with an intuitive graphical user interface for solid-state NMR data from complex protein systems

Research paper thumbnail of The POKY suite: The revolutionized platform for biomolecular studies

Research paper thumbnail of ssPINE: Probabilistic Algorithm for Automated Chemical Shift Assignment of Solid-State NMR Data from Complex Protein Systems

Membranes

The heightened dipolar interactions in solids render solid-state NMR (ssNMR) spectra more difficu... more The heightened dipolar interactions in solids render solid-state NMR (ssNMR) spectra more difficult to interpret than solution NMR spectra. On the other hand, ssNMR does not suffer from severe molecular weight limitations like solution NMR. In recent years, ssNMR has undergone rapid technological developments that have enabled structure–function studies of increasingly larger biomolecules, including membrane proteins. Current methodology includes stable isotope labeling schemes, non-uniform sampling with spectral reconstruction, faster magic angle spinning, and innovative pulse sequences that capture different types of interactions among spins. However, computational tools for the analysis of complex ssNMR data from membrane proteins and other challenging protein systems have lagged behind those for solution NMR. Before a structure can be determined, thousands of signals from individual types of multidimensional ssNMR spectra of samples, which may have differing isotopic composition...

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