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Research has been conducted on the Cellulomonas fimi 1,4-beta-glucanase CenC cellulose-binding domains. The tertiary structure of these domains has been investigated via heteronuclear magnetic resonance spectroscopy.

Research has been conducted on the mouse mammary tumor virus nucleocapsid protein. Experiments include its overexpression in Escherichia coli and purification by nuclear magnetic resonance spectroscopy.

A study was conducted to examine the interactions of the N-terminal cellulose-binding domain from Cellulomonas fimi beta-1,4-glucanase CenC with calcium by calorimetry and nuclear magnetic resonance (NMR) spectroscopy. A 50 mM sodium chloride was utilized as a buffer for the NMR studies while a line shape analysis was carried out to determine calcium kinetics. Results indicated that metal ion binding was thermodynamically correlated with native-state stability.

A study was conducted to analyze the thermal stability and oligosaccharide-binding thermodynamics of the N-terminal cellulose-binding domain of the Cellulomonas fimi endoglucanase cenC. Differential scanning calorimetry was utilized to measure stability and oligosaccharide-binding thermodynamics. Results revealed that the intramolecular link in the Cellulose fimi gene contributed to the stability of the endoglucanase cenC and a global two-dimensional minimization routine was utilized to regress the unfolding thermodynamics for the endoglucanase cenC-cellopentaose system.

The structure of the N-terminal cellulose-binding domain from Cellulomonas fimi 1,4-beta-glucanase CenC was determined by multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results revealed 10 beta-strands which were folded into two antiparallel beta-sheets, forming a jelly-roll beta-sandwich. The strands of the protein surface were shorter than those found in the opposite side of the protein, resulting in a five-stranded binding cleft containing hydrophobic residues at the center and flanked by polar hydrogen-bonding groups.

The N-terminal cellulose-binding domain (CBDN1) from Cellulomonas fimi beta-1,4-glucanase CenC binds amorphous but not crystalline cellulose. The structural and thermodynamic bases of cellulose binding were studied through NMR and difference ultraviolet absorbance spectroscopy in conjunction with calorimetry. The CBDN1 cellulose-binding site spans about five glucosyl units. The cellooligosaccharides bind along a five-stranded beta-sheet that forms a concave face of the jelly-roll beta-sandwich structure of CBDN1.

Selective isotopic labelling and 13C-NMR studies on the pK(sub a) values of the catalytic glutamic acid residues in wild type/mutant Bacillus circulans (BCX) and subtilis xylanases reveal a two-step hydrolysis mechanism involving a covalent glycosyl-enzyme intermediate. The double-displacement reaction of BCX may be broken into glycosylation and deglycosylation steps. The glycosylation step produces the glycosyl-enzyme intermediate and deglycosylation regenerates the native enzyme. These protonation and deprotonation steps are governed by glutamic ionization states.

A combined approach of NMR spectroscopy and isothermal titration calorimetry (ITC) is used for determining the ligand-binding mechanism used by a cocaine-binding aptamer. Chemical shift perturbation data and the observation of intermolecular NOEs have shown that the three-way junction is the site of ligand binding.

Evaluates the contributions of 10 amino acids within the binding cleft of one of the cellulose binding domains of the soil bacterium Cellulomonas fimi. Single site-directed mutations to alanine residues; Similar mechanism of binding to soluble and insoluble substrates; Importance of tyrosines 19 and 85 for tight binding.