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EMBELLISHMENTS ADD FUNCTIONALITY. "In addition to varied sizes, an amazing diversity of loop and domain embellishments to the basic HK97-fold increase its functionality and often provide alternate ways to stabilize the assembled particles. Particles containing subunits with the HK97-fold will undoubtedly continue to be discovered with other variations for accomplishing folding, assembly, and capsid stabilization." http://www.sciencedirect.com/science/article/pii/S0042682215001920 View in LinkedIn

Missing reference: https://lnkd.in/dXvJFtt View in LinkedIn

SIZE AND FUNCTION OF CAPSID. "The capsid size has likely evolved to accommodate the size of the material to be packaged as T. maritima encapsulins package small ferritin-like proteins inside a particle with an inner volume of 4.18×10(6) Å3 while Phage G requires a much larger capsid (inner volume=1.87×10(9) Å3) to package its 670 kb chromosome." https://lnkd.in/dXvJFtt View in LinkedIn

STRUCTURE ACROSS KINGDOMS. "The majority of capsids using the HK97-fold are of viruses infecting bacteria (bacteriophage or phage). However, this fold is also found in the coat protein floor domain of eukaryotic Herpesvirdae, including Herpes simplex virus type 1 (HSV-1), murine cytomegalovirus (MCMV), pseudorabies virus (PRV), and rhesus monkey rhadinovirus (RRV), as well as the archaeal Haloarcula sinaiiensis tailed virus 1 (HSTV-1)." View in LinkedIn

BASIC TEMPLATE. "The HK97-fold, despite sequence, structural, and functional divergences, is a basic template for formation of a proteinacious shell utilized by viruses and prokaryotic cells alike. The protein shell, composed of HK97-like subunits, serves a protective role for the genomes of viruses infecting all three domains of life. Prokaryotic cells also utilize the HK97-fold to form encapsulin nanocompartments, and possibly gene transfer agent particles that contribute to high frequencies of horizontal gene transfer." http://www.sciencedirect.com/science/article/pii/S0042682215001920 View in LinkedIn

FRAGMENT FROM NATURE continues from last weekend on the most prevalent protein fold in nature. These structures are widely used as templates for constructions across kingdoms. When mutations of these folds occur in viruses, where they originated, they result in non-infective particles. That the most plentiful life form would produce the most plentiful and flexible structures, acquired by lateral gene transfer, is probably of little surprise. View in LinkedIn

MUTATION CONSEQUENCES. "As seen with spiral polymers, scaffolding protein is important to direct threefold interactions. Interaction with scaffolding protein thus affects the geometry and imposes the correct radius of curvature, resulting in assembly of proper products with exquisite fidelity." https://lnkd.in/dXvJFtt View in LinkedIn

Travel photo of the week: bareback in Colombia https://lnkd.in/dhxD5_f View in LinkedIn

MUTATION MALWARE. "In the absence of scaffolding protein, P22 coat protein will form empty, aberrant assemblies, consisting of both hexons and pentons, such as T=4 and T=7 icosahedral capsids, or spiral structures. Similarly, mutations resulting in amino acid substitutions in coat protein that affect its flexibility or structure can influence the morphology of resulting products." http://www.sciencedirect.com/science/article/pii/S0042682215001920 View in LinkedIn

MUTANT PARTICLES. "Viral morphogenesis sometimes yields aberrant, off-pathway products. These non-infectious particles commonly arise from mutations in genes encoding structural proteins (e.g., an amber mutation in scaffolding protein or point mutations in coat protein)." http://www.sciencedirect.com/science/article/pii/S0042682215001920 View in LinkedIn