Nuclei Off the Line of Stability

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Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1.

Nuclear Magic Numbers

Li, H. Point mutations alter the mechanical stability of immunoglobulin modules. Kang, H. Stabilizing isopeptide bonds revealed in gram-positive bacterial pilus structure. Alegre-Cebollada, J. Isopeptide bonds block the mechanical extension of pili in pathogenic Streptococcus pyogenes.

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Intramolecular isopeptide bonds give thermodynamic and proteolytic stability to the major pilin protein of Streptococcus pyogenes. Reverse engineering of the giant muscle protein titin.

Strong Nuclear Force

Mechanical design of the first proximal Ig domain of human cardiac titin revealed by single molecule force spectroscopy. Carrion-Vazquez, M. Mechanical and chemical unfolding of a single protein: a comparison. USA 96 , — Randles, L. Spectrin domains lose cooperativity in forced unfolding. Perez-Jimenez, R. Mechanical unfolding pathways of the enhanced yellow fluorescent protein revealed by single molecule force spectroscopy. Soderholm, J. Importazole, a small molecule inhibitor of the transport receptor importin-beta. ACS Chem. Niopek, D. Optogenetic control of nuclear protein export.

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Record, J. Immunodeficiency and severe susceptibility to bacterial infection associated with a loss-of-function homozygous mutation of MKL1. Blood , — Beck, M. The nuclear pore complex: understanding its function through structural insight. In situ structural analysis of the human nuclear pore complex.

Bestembayeva, A. Nanoscale stiffness topography reveals structure and mechanics of the transport barrier in intact nuclear pore complexes. Surface properties determining passage rates of proteins through nuclear pores. Mohr, D. Characterisation of the passive permeability barrier of nuclear pore complexes.

Ketterer, P. DNA origami scaffold for studying intrinsically disordered proteins of the nuclear pore complex. Popa, I. Force dependency of biochemical reactions measured by single-molecule force-clamp spectroscopy. Rosa, N.

Nuclear Physics Tutorial 3

Meltdown: a tool to help in the interpretation of thermal melt curves acquired by differential scanning fluorimetry. Rodriguez, L. Wound-healing assay. Methods Mol. Download references. We thank M. Eggert and M.

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We wish to thank G. Yang for help in qPCR analysis, and C. Nichols and S. Correspondence to Sergi Garcia-Manyes. Reprints and Permissions. Advanced search.

Skip to main content. Subjects Biological physics Biophysics Chemistry Nanoscience and technology. Rent or Buy article Get time limited or full article access on ReadCube. Data availability Data supporting this research can be obtained from the corresponding author on reasonable request. References 1. This makes detailed spectroscopic studies very time-consuming, and in a number of cases even impossible. Bengtsson et a l. Scripta 29 Cheifetz et a l. Klapdor et a l. Data Nucl.

Data Tables 31 81 Kratz et a l. Physik A 43 Kratz, Nucl. A Krumlinde and P.

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  4. Larsson et a l. Nuclear stability is linked to its number of nucleons neutrons and protons. The nucleons interact with each other through the strong nuclear force, this must overcome the electrostatic repulsion between the protons to make the nucleus stable.

    When the electrostatic repulsion exceeds the strong force the nucleus is now unstable and will then change its nucleons causing radioactive decay. When the graph of number of neutrons N against protons Z is drawn, and all the stable istopes are plotted on it, there is quite a clear correlation between N and Z. This is because as the nuclear radius increases a greater strong force is required to keep it stable but adding more protons will only increase electrostatic repulsion and so the number of neutrons becomes more than that of protons.