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. 2017 Apr 6;7:691. doi: 10.1038/s41598-017-00777-6

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Secondary structure at 25 °C (a,b) and distribution of amide hydrogen temperature coefficients over the range 15°–55 °C (c) among WT () and D145E () residues. Deviation of experimental (obs.) chemical shifts (δ) from random coils for backbone C^α (a) and H^α (b). Random-coil chemical shift values were obtained from ref. 27. Rectangles (I–IV) and black line segments (αN, αA, etc) identify Ca²⁺-binding sites and α-helices known to be present in WT cTnC. Alpha-helical segments show positive deviations for C^α and negative deviations for H^α, while β-strands and loops show the opposite. Dashed lines between α-D and α-E in a and b represent the D/E linker region. In (c), amide hydrogens with temperature coefficients that were linear but very different (>95% C.I.) for WT and mutant proteins are identified by residue. Temperature coefficients of the protons coincide (or differ only slightly) for the two isoforms except where one of the paired values is labeled with an arrow.

Inline graphic — Secondary structure at 25 °C (a,b) and distribution of amide hydrogen temperature coefficients over the range 15°–55 °C (c) among WT () and D145E () residues. Deviation of experimental (obs.) chemical shifts (δ) from random coils for backbone C^α (a) and H^α (b). Random-coil chemical shift values were obtained from ref. 27. Rectangles (I–IV) and black line segments (αN, αA, etc) identify Ca²⁺-binding sites and α-helices known to be present in WT cTnC. Alpha-helical segments show positive deviations for C^α and negative deviations for H^α, while β-strands and loops show the opposite. Dashed lines between α-D and α-E in a and b represent the D/E linker region. In (c), amide hydrogens with temperature coefficients that were linear but very different (>95% C.I.) for WT and mutant proteins are identified by residue. Temperature coefficients of the protons coincide (or differ only slightly) for the two isoforms except where one of the paired values is labeled with an arrow.