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8 citations found for Lieberman, R.
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A wide variety of neutron scattering techniques can be applied to obtain information on the structure and dynamics of biological systems on multiple scales. Recent progress is summarized, as are hoped-for future developments in the context of the advent of next-generation neutron sources on various continents.
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By installing calcium-ligand triads found in olfactomedin sequences from invertebrates, insight was gained into calcium-binding features across the protein family and new surface conformations were observed that may be relevant to elusive protein–protein interactions.
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A Fab fragment with nanomolar affinity for the peptide sequence EYMPME was engineered and characterized by structural, biophysical and computational methods for potential use as a membrane-protein crystallization chaperone.
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Contrary to expectation from orthologous structures from mouse and cow, a structure of holo human adenosine deaminase 1 shows that it adopts a closed conformation at the entry to its active site. This finding poses a cautionary tale for reliance on homologs to make structural inferences relevant to applications such as protein engineering or drug development.
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Crystals of actophorin were grown in microgravity in an interactive process with astronauts on the International Space Station. Although the diffraction was not improved compared with crystals grown on Earth, a conformational change suggestive of motions intrinsic to actophorin function was observed.
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Site-directed mutants of the actin filament-severing protein actophorin were produced to improve the crystal size and diffraction limit. When 19 single mutants and a C-terminal three-residue deletion were combined into one variant, the resulting protein was significantly more thermostable and slightly more active than the wild-type protein. Larger crystals were obtained that diffracted to 1.7 Å resolution and belonged to a different space group to previous actophorin crystals.
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