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Protein Engineering - - Bog - Nova Science Publishers Inc - Plusbog.dk

New Research on Protein Synthesis - - Bog - Nova Science Publishers Inc - Plusbog.dk

Protein Water Interactions - - Bog - Nova Science Publishers Inc - Plusbog.dk

Protein Water Interactions - - Bog - Nova Science Publishers Inc - Plusbog.dk

This book is aimed at understanding which molecular parameters control the thermodynamics, structure, and functions of the protein-water systems. Proteins are one of the most important classes of biological molecules. Water binding (hydration or biological water) plays a crucial role in determining the structure, stability, and functions of proteins. Knowledge of processes occurring upon hydration or dehydration of protein macromolecules is very important in biotechnological and pharmaceutical applications of proteins such as their use as biocatalysts, biosensors, and selective adsorbents. There are essential differences between hydration and bulk water surrounding a protein. This means that a characterisation of the hydration of protein macromolecules requires elucidating the effects of both the protein on water and vice versa. Therefore, a quantitative estimation of the protein and water contributions to the thermodynamic functions of binary protein-water systems is of considerable fundamental importance and practical interest. This book describes the basic principles of a novel methodology to investigate the protein-water interactions. This methodology is based on the analysis of the excess thermodynamic functions of mixing. The thermodynamic properties (volume V, enthalpy H, entropy S, heat capacity Cp, and Gibbs free energy G) of a real binary water-protein system can be expressed in terms of the excess functions. They are the difference between the thermodynamic function of mixing in a real system and the value corresponding to an ideal system at the same temperature, pressure and composition. For an ideal system, all excess functions are zero. Deviations of the excess functions from zero indicate the extent to which the studied binary system is non-ideal due to strong specific interactions between components (ie: hydrogen bonding and charge-charge interactions).

DKK 890.00
1

Mechanical & Dynamical Principles of Protein Nanomotors - A R Khataeea - Bog - Nova Science Publishers Inc - Plusbog.dk

Mechanical & Dynamical Principles of Protein Nanomotors - A R Khataeea - Bog - Nova Science Publishers Inc - Plusbog.dk

It is obvious that movement is an essential concept of all living organisms. Molecular motility participates in many cellular functions including cell division, intracellular transport and movement of the organism itself. Thus, it is not surprising that nature has evolved a series of biological nanomotors that fulfil many of these tasks. A general class of these biological nanomotors is called protein nanomotors that move in a linear fashion (e.g. the kinesin or myosin or dynein motors) or rotate (e.g. F0F1-ATP synthase or bacterial flagellar motors). Protein nanomotors are natural motors responsible for the human activity and are also the subject of interest for nanotechnology. Protein nanomotors are ideal nanomotors because of their small size, perfect structure, smart and high efficiency. Recent advances in understanding how protein nanomotors work has raised the possibility that they might find applications as protein-based nanorobots. Thus bio-nanomotors could form the basis of bottom-up approaches for constructing active structuring and maintenance at the manometer scale. In this chapter, we have presented structures, mechanisms and potential applications of linear protein nanomotors. The three known families of protein nanomotors kinesin, dynein and myosin are multi-protein complexes and share a variety of important features. They are responsible for various dynamical processes for transporting single molecules over small distances to cell movement and growth. Our reviewing from the mechanism, regulation and co-ordination of linear nanomotors, indicate that the majority of active transport in the cell is driven by linear protein nanomotors. All of them convert the chemical energy into mechanical work directly rather than via an intermediate energy. Linear protein nanomotors are self-guiding systems. They have evolved to enable movement on their polymer filaments, either on cellular or supra-cellular levels and are able to recognise the direction of movement. Moreover, each class of nanomotor has different properties, but in the cell they are known to cooperate and even to compete with each others during their function. We have also reviewed the potential application of linear protein nanomotors. According to this, we predict that linear protein nanomotors may enable the creation of a new class of nanotechnology-based applications; for example, bio-nanorobots, molecular machines, nanomechanical devices and drug deliver systems. Thus, protein nanomotors field is very challenging field and is attracting a diverse group of researchers keen to find more.

DKK 633.00
1

The Diversified Benefits of Whey Protein - - Bog - Nova Science Publishers Inc - Plusbog.dk

Folding/Unfolding Kinetics of Lattice Proteins by Applying a Simple Statistical Mechanical Model for Protein Folding - Hiroshi Wako - Bog - Nova

Handbook on Protein Purification - - Bog - Nova Science Publishers Inc - Plusbog.dk

Handbook on Protein Purification - - Bog - Nova Science Publishers Inc - Plusbog.dk

Proteins are important biomolecules that are vital for the cellular structure and function. They perform a vast array of functions within organisms, including the catalysis of metabolic reactions, DNA replication, response to stimuli, and transporting molecules from one location to another. The technological advances in the omics areas (e.g., genomics, transcriptomics, proteomics, metagenomics, etc.) have dramatically increased the rate of discovering new proteins. Some of them hold large opportunities for innovative research and the development of commercial products and applications. It is worth noting that the global protein ingredients market is poised to grow over the next decade to reach approximately 58.49 billion USD by 2022, with the protein therapeutics market valuing around USD 315.9 billion by 2025. Interestingly, about seventy monoclonal antibody products will be on the market by 2020 with a combined worldwide sales of about 125 billion USD.The most significant parameter for the successful commercial exploitation of proteins rely on the development of an efficient and effective isolation and purification technology, known as protein downstream processing. Downstream processing refers to the technology that involves the isolation and production of purified products from natural sources such as animal tissues, plant tissues, microorganisms or fermentation broth. The most important element of this technology is the high purification processes, most important of which is chromatography and in particular affinity chromatography.This book provides information on the resent developments of protein downstream processing and deals with the information gained over the last years from the application of protein purification technologies on different research areas. Each chapter gives key examples that cover a wide range of diverse scientific disciplines in order to provide the reader with a representative sample of the current status of the field. The present book would definitely be an ideal source of scientific information to the advanced students, junior researchers, and scientists involved in cellular and molecular biology, biochemistry, microbiology, biotechnology and other related areas.

DKK 820.00
1

Protein Hydrolysates - - Bog - Nova Science Publishers Inc - Plusbog.dk

Protein Hydrolysates - - Bog - Nova Science Publishers Inc - Plusbog.dk

In this collection, the authors aim to provide information the preparation of marine protein hydrolysates and their main bioactive properties such as antioxidant, antimicrobial, antitumor and antihypertensive. Applications of these compounds in the area food technology and pharmaceuticals are also discussed.Protein Hydrolysates: Uses, Properties and Health Effects goes on to present some biological properties of fish peptides and their beneficial effects on health, emphasizing properties such as antidiabetic neuroprotective and anti-inflammatory, as a natural alternative to drugs and possible strategies to delay cognitive impairment.As confectionery manufacturers are trying to be innovative in producing suitable fat fillings for various applications. As such, the authors examine the functional, rheological and sensory properties of confectionery fat filling supplemented with different concentrations of bioactive whey protein hydrolysate powders, produced by enzymatic and microbial modification of whey proteins.Next, the bioactive potential of hydrolysate powders produced by enzymatic and microbial hydrolysis of whey proteins followed by spray drying is examined in order to determine which process allows for a highly bioactive production.A strain-substrate combination is introduced which allows for the production of dairy protein hydrolysates with high antioxidant activity and improved functional properties, which may be used as high-quality food supplements.The traditional methods for the production of functional peptides from biological sources are time-consuming and tedious. In the drug industry, it takes about five to ten years from the discovery of an industrial bioactive peptide to market delivery. To overcome the drawbacks of these traditional methods, the authors propose that a fast and versatile method is necessary.The concluding chapter presents an overview of the production and applications of bioactive peptides, demonstrating their potential use as helper agents of health processes. These peptides may aid in traditional health treatments since they can be used in high concentrations without associated toxic effects.

DKK 718.00
1

Mitogen-Activated Protein Kinases (MAPKs) - - Bog - Nova Science Publishers Inc - Plusbog.dk

Modulation of Membrane-Protein Interactions Applied to Whey Fractionation - M Carmen Almecija - Bog - Nova Science Publishers Inc - Plusbog.dk

Preferential Solvation and Hydration of Proteins in Water-Organic Mixtures - - Bog - Nova Science Publishers Inc - Plusbog.dk

Preferential Solvation and Hydration of Proteins in Water-Organic Mixtures - - Bog - Nova Science Publishers Inc - Plusbog.dk

This book describes the basic principles of a novel methodology to investigate the preferential hydration and solvation of proteins in ternary protein-water-organic solvent systems. Protein-water interactions are well-known to play a critical role in determining the function, structure, and stability of protein macromolecules. Elucidation of the processes occurring upon protein hydration in the presence of third component (organic solvents, salts, urea) is essential in a wide range of biophysical, biomedical, and biotechnological applications. In particular, there are many advantages in employing water-poor organic solvents, including the suppression of undesirable side reactions caused by water, the biocatalysis of reversed hydrolytic reactions (transesterification, peptide synthesis), or increased thermostability. Distinct intermediate protein states induced by organic solvents may be responsible for numerous neurodegenerative diseases (Alzheimer''s disease, Parkinson''s disease, and Huntington''s disease). However, the manner in which organic solvents increase/decrease the thermal stability, induce/reduce the extent of denaturation, and stabilise/destabilise the partially folded conformations of proteins (amyloid fibrils and molten globules) is an intricate function of water content in organic liquids. Preferential hydration/solvation is an effective method for revealing the mechanism of the protein stabilisation or denaturation. When a protein interacts with a binary water-organic solvent mixture, the three components do not equally mix. Water or organic solvent molecules exist preferentially in the protein''s solvation shell. This difference between the solvation shell and bulk solvent in the solvent components has been termed preferential solvation. Preferential solvation is a thermodynamic quantity that describes the protein surface occupancy by the water and cosolvent molecules. This is associated with the actual numbers of water/cosolvent molecules that are in contact with the protein''s surface. It was also found that the protein destabilisation is directly associated with the preferential binding of the denaturant molecules to specific protein groups. The aim of our study is to monitor the preferential solvation and preferential hydration of the protein macromolecules at low, intermediate, and high water content in organic solvents at 25 oC. Our approach is based on the simultaneous measurements of the absolute values of the water and organic solvent sorption. The preferential solvation/hydration parameters were calculated using the water and organic solvent sorption values. The preferential solvation/hydration parameters were compared with the corresponding changes in the protein structure that transpire regarding the interaction of the protein with organic solvent and water molecules. The effect of organic solvent on the protein structure was investigated by FTIR (Fourier Transform Infrared) spectroscopy.

DKK 718.00
1

A Closer Look at Membrane Proteins - - Bog - Nova Science Publishers Inc - Plusbog.dk

Proteomics - - Bog - Nova Science Publishers Inc - Plusbog.dk

Bioencapsulation in Silica-Based Nanoporous Sol-Gel Glasses - Farid Menaa - Bog - Nova Science Publishers Inc - Plusbog.dk

Molecular Pathology of Proteins - - Bog - Nova Science Publishers Inc - Plusbog.dk

HSP70s - - Bog - Nova Science Publishers Inc - Plusbog.dk

Foldases Catalyzing the Formation & Isomerization of Disulfide Bonds in Proteins - Natalya K Nagradova - Bog - Nova Science Publishers Inc -

Foldases Catalyzing the Formation & Isomerization of Disulfide Bonds in Proteins - Natalya K Nagradova - Bog - Nova Science Publishers Inc -

One of the rate-limiting steps in the folding pathways of many secretory proteins is the formation of correct disulfide bonds between cysteine residues. In eukaryotes, both disulfide bond formation and isomerisation which shuffles incorrectly formed disulfides are catalysed by protein disulfide isomerase (PDI), whereas in bacteria these two reactions are catalysed by separate enzymes. Both in eukaryotic and prokaryotic cells the oxidation and isomerisation steps proceed exclusively in extracytoplasmic environments (the lumen of the eukaryotic endoplasmic reticulum and the Gram-negative bacterial periplasmic space). The family of foldases under discussion is characterised by a conserved "thioredoxin fold" and a common active site motif: Cys-X-X-Cys. The process of disulfide bond formation relies on thiol-disulfide exchange between oxidised and reduced cysteine pairs in the catalyst and substrate protein. Two separate pathways involved in disulfide bond formation and isomerisation have been characterised both in eukaryotes and in bacteria. In the oxidative pathway, oxidizing equivalents flow from oxygen to a membrane protein (Ero1p in eukaryotes or DsbB in bacteria), and then to a folding protein containing reduced cysteines via PDI (in eukaryotes) or via DsbA (in bacteria). In the isomerisation pathway, DsbC (bacterial protein disulfide isomerase) or PDI (in eukaryotes) interacts with substrate proteins that contain non-native disulfide bonds, allowing these bonds to rearrange to their native pairings. Reducing equivalents which are necessary to maintain DsbC in a reduced form, able to attack misfolded disulfides, are transferred from the cytoplasm with the aid of the cytoplasmic membrane protein DsbD. In eukaryotes, reduced glutathione is the main source of reducing equivalents for PDI. A dual role of PDI as an oxidase and an isomerase is facilitated by its complex domain architecture.

DKK 405.00
1

Protein Kinase C - - Bog - Nova Science Publishers Inc - Plusbog.dk

Novel Enzyme / DNA Inorganic Materials - Chall V Kumar - Bog - Nova Science Publishers Inc - Plusbog.dk

Surface Plasmon Resonance (SPR) - - Bog - Nova Science Publishers Inc - Plusbog.dk

Surface Plasmon Resonance - Pranveer Singh - Bog - Nova Science Publishers Inc - Plusbog.dk

Phage Display as a Tool for Synthetic Biology - Santina Carnazza - Bog - Nova Science Publishers Inc - Plusbog.dk

Handbook on Estrogen Receptors in the Brain - Vijay Paramanik - Bog - Nova Science Publishers Inc - Plusbog.dk

Macromolecular Chemistry - - Bog - Nova Science Publishers Inc - Plusbog.dk