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Aim: To explore undergraduate nursing students' understanding of fundamental care and identify educational leadership opportunities to deepen students' understanding of fundamental care concepts. Design: Sequential‐explanatory mixed methods study. Methods: We conducted a cross sectional survey (n = 202) and focus groups (n = 24) to explore undergraduate nursing students' ability to identify fundamental care needs. All data were collected between November 2020 and April 2021. Survey data were analysed using descriptive and inferential statistics and focus group data were thematically analysed. Results: Year One students scored significantly lower in their ability to identify fundamental care needs compared with students in other years, even after controlling for route, gender and age. Post‐degree students scored significantly higher than direct entry or transfer students. Students ≤19 years of age had significantly lower scores compared with students ≥25 years of age. Our focus group findings highlighted that students were often unable to define fundamental care, but they identified learning about various components of fundamental care in a variety of ways. While students understood that fundamental care was required in all settings, they were challenged in providing this care in acute and virtual settings. Students shared several suggestions to support fundamental care skills development across the curriculum. Conclusions: There is a need for a clear definition and description of the fundamentals of care that is used consistently by faculty, students and curriculum documents. It is important to encourage and support educators to share real‐world nursing stories, offer students time to share their personal experiences, develop creative learning opportunities and foster student reflection to deepen students' understanding of the fundamentals of care. Impact Educators need support to meaningfully incorporate fundamentals of care learning opportunities across multiple care settings. Educational leaders can use these findings to develop or adapt their curricula to support fundamental care skill development. [ABSTRACT FROM AUTHOR]

The recognition of RNA by human U1A protein combined with [super 13]C relaxation studies have shown little changes in the protein-binding site, but the upper stem-loop of RNA has experienced free movement. This increased flexibility in the presence of protein has indicated optimum intermolecular contacts in protein-RNA complex.

To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.tibs.2006.06.002 Byline: Zahra Shajani (1), Pritilekha Deka (1), Gabriele Varani (1)(2) Abstract: When proteins and small molecules bind to RNA, they often alter its conformation. These structural changes are an essential aspect of the ability of RNA to sense signaling molecules and modulate gene expression. Thus far, few studies have been dedicated to understanding how RNA moves at a residue level and how these motions change upon complex formation. A recent report highlights how intrinsic motions in RNA correlate with its ability to bind to cognate ligands. Author Affiliation: (1) Department of Chemistry, University of Washington Seattle, WA 98195-1700, USA (2) Department of Biochemistry, University of Washington Seattle, WA 98195-1700, USA

The local disorder at individual RNA nucleotides as quantified by the generalized order parameter ([S.sup.2]) has correlated strongly with SHAPE (selective 2'-hydroxyl acylation analyzed by primer extension) reactivities but not with solvent accessibility. SHAPE has measured spatial disorder and structural dynamics at single nucleotide resolution in RNA.

An extensive set of [super 13]C NMR relaxation parameters were used to study the dynamics of the double-stranded DNA target of the HhaI methyltransferase. The deoxycytidine ribose moieties are found to be more mobile than other nucleotides and all of the nucleotides within the HhaI recognition site exhibited anomalous base dynamics.

The dynamics of the phosphodiester backbone in the [[5'-GCGC-3'].sub.2] moiety of the DNA oligomer are analyzed by using deuterium solid-state NMR (SSNMR). The NMR data has shown that the [[5'-GCGC-3'].sub.2] moiety is dynamic and the change of orientation of this moiety in DNA upon methylation has made the molecule less amenable to binding to the HhaI endonuclease.

A deuterium solid-state NMR (SSNMR) was used to study the dynamics of the furanose rings in the GCGC moiety of the DNA oligomer [[d([G.sub.1][A.sub.2][T.sub.3][A.sub.4][G.sub.5][C.sub.6][G.sub.7][C.sub.8][T.sub.9][A.sub.10][T.sub.11][C.sub.12])].sub.2]. The NMR data results shed light onto the dynamic property of 5'-GCGC-3' with the largest-amplitude motions occurring nearest the methylation site and its structural rearrangements when the DNA binds to the Hhal methyltransferase.

The site-specific [super 2]H solid-state NMR study of RNA dynamics is described. The results in both DNA and RNA have shown that the [micro]s-ns is rich in proteins as it is in nucleic acids.

Solid state and solution NMR are used to investigate internal motions at six positions near the HhaI methyltransferase enzyme recognition site for the [[5'-(dGATAGCGCTATC)-3'].sub.2] DNA dodecamer. The results have shown that the HhaI DNA methylation target site possesses an intrinsically dynamic structure and the measurements of dynamics for many nucleotides in the vicinity of the methylation site have identified two residues that experience significant mobility in the absence of the methylase.

The goal of this work was to examine if sequence-dependent conformational flexibility in DNA plays a role in base extrusion, a common conformational change induced by many DNA-modifying enzymes. We studied the dynamics of the double-stranded DNA target of the HhaI methyltransferase by recording an extensive set of 13C NMR relaxation parameters. We observe that the cytidine furanose rings experience fast (picosecond to nanosecond) motions that are not present in other nucleotides; .the methylation site experiences particularly high mobility. We also observe that the bases of guanosine and cytidine residues within the HhaI recognition sequence GCGC experience motions on a much slower (1-100 µs) time scale. We compare these observations with previous solution and solid-state NMR studies of the EcoRI nuclease target sequence, and solid-state NMR studies of a similar HhaI target construct. While an increased mobility of cytidine furanose rings compared to those of other nucleotides is observed for both sequences, the slower motions are only observed in the HhaI target DNA. We propose that this inherent flexibility lowers the energetic barriers that must occur when the DNA binds to the HhaI methyltransferase and for extrusion of the cytidine prior to its methylation. [ABSTRACT FROM AUTHOR]

Recognition of RNA by proteins and small molecules often involves large changes in RNA structure and dynamics, yet very few studies have so far characterized these motional changes. Here we extend to the protein-bound RNA recent 13C relaxation studies of motions in the RNA recognized by human UIA protein, a well-known model for protein-RNA recognition. Changes in relaxation observed upon complex formation demonstrate that the protein-binding site becomes rigid in the complex, but the upper stem-loop that defines the secondary structure of this RNA experiences unexpected motional freedom. By using a helix elongation strategy, we observe that the upper stem-loop moves independently of the remainder of the structure also in the absence of UIA. Surprisingly, RNA residues making important intermolecular contacts in the structure of the complex exhibit increased flexibility in the presence of the protein. Both of these results support the hypothesis that RNA-binding proteins select a structure that optimizes intermolecular contacts in the manifold of conformations sampled by the free RNA and that protein binding quenches these motions. Together with previous studies of the RNA-bound protein, they also demonstrate that protein-RNA interfaces experience complex motions that modulate the strength of individual interactions. [ABSTRACT FROM AUTHOR]

The widespread importance of induced fit and order–disorder transition in RNA recognition by proteins and small molecules makes it imperative that RNA motional properties are characterized quantitatively. Until now, however, very few studies have been dedicated to the systematic characterization of RNA motion and to their changes upon protein or small-molecule binding. The U1A protein–RNA complexes provide some of the best-studied examples of the role of RNA motional changes upon protein binding. Here, we report 13C NMR relaxation studies of base and ribose dynamics for the RNA internal loop target of human U1A protein located within the 3′-untranslated region (3′-UTR) of the mRNA coding for U1A itself. We also report the semi-quantitative analysis of both fast (nano- to picosecond) and intermediate (micro- to millisecond) motions for this paradigmatic RNA system. We measure 13C T 1, T 1ρ and heteronuclear nuclear Overhauser effects (NOEs) for sugar and base nuclei, as well as the power dependence of T 1ρ at 500MHz and 750MHz, and analyze these results using the model-free formalism. The results provide a much clearer picture of the type of motions experienced by this RNA in the absence of the protein than was provided by the analysis of the structure based solely on NOEs and scalar couplings. They define a model where the RNA internal loop region ”breathes” on a micro- to millisecond timescale with respect to the double-helical regions. Superimposed on this slower motion, the residues at the very tip of the loop undergo faster (nano- to picosecond) motions. We hypothesize that these motions allow the RNA to sample multiple conformations so that the protein can select a structure within the ensemble that optimizes intermolecular contacts. [Copyright &y& Elsevier]

RNA and DNA molecules experience motions on a wide range of time scales, ranging from rapid localized motions to much slower collective motions of entire helical domains. The many functions of RNA in biology very often require this molecule to change its conformation in response to biological signals in the form of small molecules, proteins or other nucleic acids, whereas local motions in DNA may facilitate protein recognition and allow enzymes acting on DNA to access functional groups on the bases that would otherwise be buried in Watson-Crick base pairs. Although these statements make a compelling case to study the sequence dependent dynamics in nucleic acids, there are few residue-specific studies of nucleic acid dynamics. Fortunately, NMR studies of dynamics of nucleic acids and nucleic acids-protein complexes are gaining increased attention. The aim of this review is to provide an update of the recent progress in studies of nucleic acid dynamics by NMR based on the application of solution relaxation techniques.