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• W1736530025 abstract "Investigation of the Thermodynamic Properties of the Oligomerization Domain of Heterogeneous Nuclear Ribonucleoprotein C by John Patrick O’Brien III The heterogeneous nuclear ribonucleoprotein C (hnRNP C) performs a critical role in the processing of nascent pre-messenger ribonucleic acid (pre-mRNA) transcripts as they exit DNA polymerase II. As the pre-mRNA transcripts emerge from the polymerase complex, they are bound by hnRNP C only if its nucleotide (NT) chain is longer than a certain nucleotide length. If the chain is long enough and binding occurs, the nucleotide strand is exported and processed as mRNA, whereas if the length requirement is not met, the RNA sequence is directed along a pathway to become small nuclear RNA (snRNA). The functional form of hnRNP C is a four-copy tetramer, with four C proteins associating at their leucine zipper-like oligomerization domains (CLZ) to form the complex. The CLZ domains form a coiled-coil tetramer, a very stable structural motif in biological macromolecules. This work studies the thermodynamic properties of the CLZ domain of hnRNP C. Fluorescence resonance energy transfer (FRET) assays were conducted using fluorescently labeled CLZ peptides to determine the equilibrium dissociation constant (KD) as well as the rate of tetramer formation (kon). The experimental data was used in conjunction with computational simulations to gain a more coherent picture of CLZ interactions." @default.
• W1736530025 created "2016-06-24" @default.
• W1736530025 creator A5032794444 @default.
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• W1736530025 date "2015-01-01" @default.
• W1736530025 modified "2023-09-27" @default.
• W1736530025 title "Investigation of the thermodynamic properties of the oligomerization domain of heterogeneous nuclear ribonucleoprotein c" @default.
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• W1736530025 hasPublicationYear "2015" @default.
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