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Methods for rapidly assessing sequence-structure-function landscapes and developing conditional gene-regulatory devices are critical to our ability to manipulate and interface with biology.
To further assess sequence motifs and propensity for secondary structure and solvent exposure states for all (and not only structurally resolved) SNO proteins, we used sequence-based analysis and prediction methods.
In recent years, new, so-called structurally constrained (SC) models of protein-coding sequence evolution have been proposed, which use statistical potentials to assess sequence-structure compatibility.
Multiple sequence alignment is often used to assess sequence conservation of protein domains, tertiary and secondary structures, and even individual amino acids or nucleotides.
Specifically, similarity of binding sites is assessed by considering the sites' sequence and structure conservation as well as physicochemical properties of protein assemblies.
P.-S.H., K.F., B.H. and D.B. collected and analyzed sequence and structure comparison data.
Extended Data Fig. 6 Sequence and structure conservation of Cx46 and Cx50 heteromeric/heterotypic interfaces.
Supplementary Figure 2 Sequence and structure of bio-Pup(E) and bio-DE28.
Lee, D., Redfern, O. & Orengo, C. Predicting protein function from sequence and structure.
Mun, J.-H. et al. Sequence and structure of Brassica rapa chromosome A3.
Compared to human or mouse, the sequence and structure of rat lncRNAs are less identified.
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