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[NMR paper]
Structural Model of Bacteriophage P22 Scaffolding Protein in a Procapsid by Magic-Angle Spinning NMR
Structural Model of Bacteriophage P22 Scaffolding Protein in a Procapsid by Magic-Angle Spinning NMR
Icosahedral dsDNA viruses such as the tailed bacteriophages and herpesviruses have a conserved pathway to virion assembly that is initiated from a scaffolding protein driven procapsid formation. The dsDNA is actively packaged into procapsids, which undergo complex maturation reactions to form infectious virions. In bacteriophage P22, scaffolding protein (SP) directs the assembly of coat proteins into procapsids that have a T=7 icosahedral arrangement, en route to the formation of the mature...
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[NMR paper]
NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Nuclear magnetic resonance (NMR) spectroscopy allows studying proteins in solution and under physiological temperatures. Frequently, either the amide groups of the protein backbone or the methyl groups in side chains are used as reporters of structural dynamics in proteins. A structural dynamics study of the protein backbone of globular proteins on ^(15)N labeled and fully protonated samples usually works well for proteins with a molecular weight of up to 50 kDa. When side...
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[NMR paper]
Investigation of Protein Therapeutics in Frozen Conditions Using DNP MAS NMR: A Study on Pembrolizumab
Investigation of Protein Therapeutics in Frozen Conditions Using DNP MAS NMR: A Study on Pembrolizumab
The success of modern biopharmaceutical products depends on enhancing the stability of protein therapeutics. Freezing and thawing, which are common thermal stresses encountered throughout the lifecycle of drug substances, spanning protein production, formulation design, manufacturing, storage, and shipping, can impact this stability. Understanding the physicochemical and molecular behaviors of components in biological drug products at temperatures relevant to manufacturing and shipping...
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[NMR paper]
NMR and molecular simulation studies on the structure elucidation of the amphotericin B ion channel using (13)C and (19)F labelling
NMR and molecular simulation studies on the structure elucidation of the amphotericin B ion channel using (13)C and (19)F labelling
Amphotericin B (AmB) has been clinically used for serious fungal infections for over 60 years. The drug is characterized by its specific recognition of ergosterol (Erg) in the fungal cell membrane. AmB and Erg form an ion-channel assembly, which is thought to play a major role in the antibiotic activity of AmB. The precise structure of the ion channel in fungal membranes still remains unelucidated. Recently, the structure of an AmB assembly formed in...
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