Solid-state NMR (ssNMR) is uniquely suited for determining the distance between pairs of isotopically labeled atoms at the protein-surface interface ( Goobes et al., 2007). While many experimental methods exist for studying proteins adsorbed to solid surfaces, most can only resolve macroscopic features ( Gray, 2004). The structure of biomineral-associated proteins cannot be determined by X-ray crystallography or solution NMR as a result, high-resolution aspects of protein biomineralization are not well understood. Deleterious biomineralization can result in pathologies such as kidney stones ( Dussol et al., 1995 Ryall, 1996), dental calculus, and atherosclerosis ( Dorozhkin and Epple, 2002). Some common biogenic materials include calcified minerals, magnetite, and biosilica. These include a variety of structural and functional materials and the mineral phase of hard tissues. Many organisms utilize biomineralization to fabricate the solid inorganic components of biogenic materials. During crystal growth, proteins can locate and function at the liquid-solid surface phase boundary and accelerate ( Elhadj et al., 2006), inhibit ( Boskey et al., 1993 Shiraga et al., 1992), or shape crystal growth ( Naka and Chujo, 2001 Sollner et al., 2003). This method is generally applicable to proteins that can be chemically synthesized.īiomineralization is a process of crystal nucleation and growth controlled by bioorganic molecules such as proteins ( Dove P. The work represents a significant advance toward determining structure of biomineral-adsorbed protein using experimentally biased structure prediction. Computation and experiment converge on an ensemble of related structures and identify preferential binding at three crystal surfaces. We use this new method to determine most of the structure of human salivary statherin interacting with the mineral phase of tooth enamel. In addition, the algorithm is able to identify lattice geometries most compatible with ssNMR constraints, representing a quantitative, novel method for investigating crystal-face binding specificity. The method combines solid-state NMR (ssNMR) and ssNMR-biased computational structure prediction. Here we report a method for determining the structure of biomineral-associated proteins. Unfortunately, the structure of biomineral-associated proteins cannot be determined by X-ray crystallography or solution NMR. All rights reserved.Protein-biomineral interactions are paramount to materials production in biology, including the mineral phase of hard tissue. IMPORTANT: You must include your IP address, otherwise we won't know which address to unblock! You can check your actual IP address (as seen by the outside world) using a free service such as Ĭopyright © 2022 CrystalMaker Software Ltd. Please contact us to request that we unblock your access. Have we made a mistake? If you believe we have mistakenly blocked your access, we apologise. You, or another user with the same IP address, has been detected posting spam, attempting to hack this site, or making a denial-of-service attempt. So please purchase the appropriate licence(s) from us, and delete any stolen software from your computer. Without this income there would be no software. We rely on software sales to fund our research and development. You, or another user with the same IP address, has been detected using an illegal, stolen ("hacked") copy of our software.ĭo not use stolen or "hacked"/"cracked" software: it's illegal - and it's seriously uncool: nobody likes a cheat. Access Denied You are forbidden to access this website because: Either:
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