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- W1981292543 abstract "Telomeres are complex nucleoprotein structures, formed at the ends of linear chromosomes as means of termini protection and stabilization. They were developped in response to the so-called termini replication problem, which caused steady shortening of Eukaryota chromosomes over the course of cell divisions. In numerous species, including humans, telomeric DNA consists of tandem 5'-TTAGGG-3' repeats of various length (ca. 10 kbp in case of human chromosomes); this portion of non-coding DNA can be lost during proliferation with no loss in genetic information. Constitutively proliferating cells, however, need to produce telomerase -- a ribonucleoprotein which is able to elongate the termini by use of its own RNA template. Telomere-deficient chromosomes might undergo ligation by cellular mechanisms of DNA repair and, further, trigger apoptosis; at the same time, telomere shortening is considered to be a cellular marker of aging. These two reasons make telomeres subject to particular attention in fields of drug design and senescence research.The telomere structure is stabilized by a number of distinct proteins, building up the shelterin complex. Two of these are responsible for specifically recruiting the complex to the telomeric sequence: Telomere repeat-binding factors 1 and 2 (TRF1 and TRF2). Here we present a detailed comparative Molecular Dynamics study of their mechanism of binding and sequence recognition. A decomposed free energy profile is used to quantify the key determinants of binding. We reproduce the experimental affinity data on the fully atomic scale, and propose a novel mechanism of sequence specificity. Moreover, we have computed a 2D PMF profile that enables us to draw conclusions about the association-dissociaton dynamics." @default.
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- W1981292543 date "2014-01-01" @default.
- W1981292543 modified "2023-09-30" @default.
- W1981292543 title "Mechanisms of Trf1/Trf2 Binding Properties and DNA Sequence Recognition as Studied by Molecular Dynamics" @default.
- W1981292543 doi "https://doi.org/10.1016/j.bpj.2013.11.3856" @default.
- W1981292543 hasPublicationYear "2014" @default.
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