Protein electrostatics: From computational and structural analysis to discovery of functional fingerprints and biotechnological design

Protein electrostatics: From computational and structural analysis to discovery of functional fingerprints and biotechnological design

Computing driven protein engineering aims to enable them to withstand an extended range of conditions and to mediate modified or novel functions. Therefore, it is very important for industrial biotechnology, biomedical and pay for new challenges in environmental science, such as biocatalysis for green chemistry and bioremediation.

To achieve this goal, it is important to clarify the molecular mechanisms underlying the stability of proteins and modulate their interactions. So far, much attention has been given to the packing of hydrophobic and polar interactions and the stability of the protein core.

Instead, the role of electrostatics and, in particular, surface interactions has received less attention. However, electrostatics plays an important role throughout the entire life cycle of proteins, because the initial folding steps to maturation, and is involved in the regulation of protein localization and interaction with cellular or other artificial molecule. Short and long-range electrostatic interactions, together with other forces, provide important guidance cues in the assembly of molecules and macromolecules.

We report here on a method for calculating electrostatic and for analysis of individual proteins or protein capable comparison sort by electrostatic similarity. Then, we give examples of electrostatic and fingerprint analysis in the evolution of the natural protein in the design and biotechnology, in areas as diverse as biocatalysis, antibodies and nanobody engineering, drug design and delivery, molecular virology, nanotechnology and regenerative medicine.
Biomimetic has emerged as a multi-disciplinary knowledge in several subjects biomedicine in recent decades, including biomaterials and dentistry.

In restorative dentistry, biomimetic approach has been applied to a variety of applications, such as restoring defective teeth using bioinspired peptides to achieve remineralization, bioactive and biomimetic biomaterials, and tissue engineering for regeneration. Advances in modern adhesive restorative materials, understanding the biomaterial-tissue interaction at the nano and micro further improved restorative material properties (such as color, morphology, and strength) to mimic natural teeth.

 Protein electrostatics: From computational and structural analysis to discovery of functional fingerprints and biotechnological design
Protein electrostatics: From computational and structural analysis to discovery of functional fingerprints and biotechnological design

Evaluating the spectral overlap with the cooling rate in UCP luminescence energy transfer system

The use of organic fluorophores based on well-established as a key tool in the biological sciences, with many biological-sensing method takes advantage of Forster Resonance Energy Transfer (FRET) between fluorescent organic dyes based on the following different one photon excitation.

However, work by absorbing UV-visible dyes as fluorescent tags and markers typically suffer from several drawbacks including relatively high energy excitation wavelengths, and autofluorescence competitive photobleaching, which often limit their effectiveness and longevity both in vitro and in vivo.

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As an alternative, the lanthanide doped upconverting phosphor (UCP) has emerged as a new class of materials for use in optical imaging and sensing RET; they show photographs and high chemical stability and utilizing near infrared excitation. Approaches to sense the target analyte is given employing upconverting phosphors can be achieved by engineering the UCP to operate an analog to a fluorescent dye through Luminescence Resonance Energy Transfer (LRET) and the system as it is now at the center of optical sensing low concentration of important biological species and distance measurement.

Sean

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