linkedin post 2017-08-27 06:39:11

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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
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linkedin post 2017-08-26 05:59:02

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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
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linkedin post 2017-08-27 06:36:31

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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
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linkedin post 2017-08-27 06:32:07

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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
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linkedin post 2017-08-27 06:28:32

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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
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linkedin post 2017-08-26 06:27:43

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FLEXIBILITY VERSUS STABILITY. "Conformational flexibility is also necessary for the rearrangements during the capsid maturation process. Thus, a fine balance is necessitated between this conformational polymorphism and stability of monomeric coat proteins." http://www.sciencedirect.com/science/article/pii/S0042682215001920 View in LinkedIn
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linkedin post 2017-08-26 06:23:15

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VERSATILE LEGO. "For most capsids with HK97-like coat proteins, chemically identical subunits occupy non-identical sites in the icosahedron. This relies on coat protein plasticity as well as a mechanism by which identical subunits can be “switched” into slightly different conformations required to occupy quasi-equivalent sites in the icosahedron, a process known as conformational switching." http://www.sciencedirect.com/science/article/pii/S0042682215001920 View in LinkedIn
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linkedin post 2017-08-26 06:21:08

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CAPSID β-HINGE OF P22. "This hinge appears to direct motion of the A-domain during hexon symmetrization that occurs simultaneously with expansion. Finally, plug proteins (gp4, gp10 and gp26) close the portal protein channel and tailspike proteins (gp9) are added to complete the mature infectious phage." http://www.sciencedirect.com/science/article/pii/S0042682215001920 View in LinkedIn
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