The Stereo-Array Isotope Labeling (SAIL) method has been successfully applied for structure determinations of proteins as large as 50 kDa, which are unamenable to conventional NMR methods.(1) In view of the recent trend of integrative structural biology research, the major role of NMR spectroscopy has shifted from structure determinations to elucidations of the dynamics and interactions of biologically interesting large protein complexes. The relaxation optimized SAIL approach will facilitate various investigations of protein dynamics with wider amplitudes and time-scale ranges for large protein complexes. Our recent results along this line will be presented.(2,3
Although NMR spectroscopy is usually employed for structural studies of relatively small proteins, t...
Structural studies of proteins are critical for understanding biological processes at the molecular ...
The prevailing dogma in structural genomics is the existence of a strong correlation between protein...
The size of macromolecular structures that can be solved by nuclear magnetic resonance (NMR) spectro...
Traditionally, the major obstacle to using NMR spectroscopy to gain meaningful structural informatio...
International audienceOverwhelming evidence now illustrates the defining role of atomic-scale protei...
Nuclear magnetic resonance (NMR) spectroscopy is a powerful method for the study of the structure, d...
NMR spectroscopy is a key method for studying the structure and dynamics of (large) multidomain prot...
Biological activity in the cell is predominantly mediated by large multiprotein and protein-nucleic ...
This chapter reviews current state-of-the-art NMR approaches for studying the structure and dynamics...
Abstract In order to compare high resolution crystal structures of proteins with the corresponding s...
Dynamics are intimately linked to protein stability and play a crucial role in important biological ...
Proteins are the molecular machines of a cell and are involved in virtual all cellular processes. To...
NMR structural investigations of water-soluble proteins are well established in biological and bioch...
A novel NMR experiment for obtaining sequential assignment of large proteins and protein complexes i...
Although NMR spectroscopy is usually employed for structural studies of relatively small proteins, t...
Structural studies of proteins are critical for understanding biological processes at the molecular ...
The prevailing dogma in structural genomics is the existence of a strong correlation between protein...
The size of macromolecular structures that can be solved by nuclear magnetic resonance (NMR) spectro...
Traditionally, the major obstacle to using NMR spectroscopy to gain meaningful structural informatio...
International audienceOverwhelming evidence now illustrates the defining role of atomic-scale protei...
Nuclear magnetic resonance (NMR) spectroscopy is a powerful method for the study of the structure, d...
NMR spectroscopy is a key method for studying the structure and dynamics of (large) multidomain prot...
Biological activity in the cell is predominantly mediated by large multiprotein and protein-nucleic ...
This chapter reviews current state-of-the-art NMR approaches for studying the structure and dynamics...
Abstract In order to compare high resolution crystal structures of proteins with the corresponding s...
Dynamics are intimately linked to protein stability and play a crucial role in important biological ...
Proteins are the molecular machines of a cell and are involved in virtual all cellular processes. To...
NMR structural investigations of water-soluble proteins are well established in biological and bioch...
A novel NMR experiment for obtaining sequential assignment of large proteins and protein complexes i...
Although NMR spectroscopy is usually employed for structural studies of relatively small proteins, t...
Structural studies of proteins are critical for understanding biological processes at the molecular ...
The prevailing dogma in structural genomics is the existence of a strong correlation between protein...