The separation line (also called ‘Yin-Yang’ diameter) formed by two semicircles of the ‘Tai-Chi’ symbol generate more binary interaction than does the linear diameter. The architecture of homodimeric Sso7c4 is presented as the Chinese traditional ‘Tai-Chi’ symbol. These arrangements form a strand-switched dimer interface. In addition, another short β-sheet is constructed by the β2 strand from each monomer. Association of the monomers is through two β-sheets in each sheet, two strands derive from one monomer and the first strand forms the other monomer. The two monomers are colored differently for clarity. ( D) The individual secondary structure elements are indicated in the ribbon diagram. ( C) NMR ensemble of the selected structures is shown with a backbone chain. ( B) Topology diagram of the Sso7c4 structure showing the connectivity between strands in two β-sheets. The amide protons with very slow exchange rates are circled. Long-range NOEs between β-strands are indicated by double arrows. Heteronuclear single quantum coherence (HSQC) spectroscopy is one of the work horses in that field often used to map structural connectivity between protons and carbons or other hetero. ( A) The proton nuclear Overhauser enhancement (NOE) networks of the swapped six-stranded and the short two-stranded antiparallel β-sheets of Sso7c4 are defined from the NOEs and amide exchange rate. Topology and NMR structure of the dimeric Sso7c4 protein. furiosus TK, Thermococcus kodakaraensis PHS, P. The scale bar indicates the distance corresponding to 0.1 amino acid substitutions per site. The protein names are colored according to the classification as in (A). ( B) The phylogenetic tree for the above alignment. The residues R11 and R22 are highly conserved across the species and other hydrophobic residues are also important in hydrophobic interactions. Residues are numbered according to Sso7c4a from S. For the group I (Sso7c3, Sso7c4, Saci0101, Saci1212 and STS096) and the group 2, each possessing shorter sequence length near 55 and 75 amino acids, respectively, are aligned. Sequences were obtained form the National Center for Biotechnology Information database ( ). The alignment was performed with the T-coffee server (30). ( A) Sequence alignment of the Sso7c4 family from several archaeas with the corresponding secondary structural elements noted. The resulting spectrum is two-dimensional with one axis for 1 H and other for a heteronuclear most often 13 C or 15 N. This technique is applied in complex biofluid samples that are used for high throughput metabolomics studies and shows promise of better information recovery than conventional two-dimensional NMR technique in shorter time.Comparison of Primary Sequences of Sso7c4 protein family in Archaeal kingdom. The HSQC (Heteronuclear Single Quantum Coherence) experiment is used frequently in NMR spectroscopy of organic molecules and is of particular significance in the field of protein NMR. Graphical abstract SOFAST-HMQC is a two-dimensional NMR technique that significantly decreases experimental time without loss of information. Hence, this can be used for high throughput study. This technique takes sevenfold less experimental time than the conventional 1H- 13C HSQC experiment with retention of almost all molecular information. We have reported the application of selective optimized flip angle short transient (SOFAST) technique coupled to heteronuclear multiple quantum correlation (HMQC) along with nonlinear sampling (NUS) in urine and serum samples. This makes it almost impossible to be used in high throughput study. However owing to poorer natural abundance and gyromagnetic ratio of 13C, the acquisition time for 2D 1H- 13C heteronuclear single quantum coherence spectroscopy (HSQC) is long. In order to circumvent this problem, 2D 1H- 13C correlation spectroscopy techniques are often used. Nuclear magnetic resonance (NMR)-based metabolomics relies mostly on 1D NMR however, the technique is limited by overlap of the signals from the metabolites.
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