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Occurrence, Functions and Biological Significance of Arginine-Rich Proteins.

E-mail: [email protected] Received Date: July 01, ; Accepted Date: September 28, ; These components interact with each other resulting in various functions such as taste, digestion [3,4], protection, lubrication [5,6], cleaning, buffering capacity [3] and maintaining integrity of the tooth structure [6]. Retinol-binding proteins (RBP) are a family of proteins with diverse functions. E -mail: [email protected] Received date: 25/05/; Accepted date: 24/12/; Published date: 29/12/ An in silico study has been performed for 3D structure prediction and molecular phylogenetic analysis of RBP from two . 18 of the most unusual questions asked on Yahoo Answers.

A protein's shape forms from complex interactions between the amino acids that make up the protein chain and between the amino acids and the surrounding environment. Ultimately, the protein assumes the shape that best balances out all these factors so that the protein achieves the lowest possible energy state. The Rosetta program used by Lu and his colleagues can predict the structure of a protein by taking into account these interactions and calculating the lowest overall energy state.

It is not unusual for the program to create tens of thousands of model structures for an amino acid sequence and then identify the ones with lowest energy state.

Protein Map Standardization of Human Saliva Using Two Dimensional Gel Electrophoresis (2-DE)

The resulting models have been shown to accurately represent the structure the sequence will likely assume in nature. Determining the structure of transmembrane proteins is difficult because portions of transmembrane proteins must pass though the membrane's interior, which is made of oily fats called lipids. In aqueous fluids, amino acid residues that have polar sidechains - components that can have a charge under certain physiological conditions or that participate in hydrogen bonding -- tend to be located on the surface of the protein where they can interact with water, which has negatively and positively side charges to its molecule.

As a result, polar residues on proteins are called hydrophilic, or "water-loving. Such residues are called hydrophobic or "water-fearing. In membranes, however, protein folding is more complicated because the lipid interior of the membrane is non-polar, that is, it has no separation of electrical charges.

This means to be stable the protein must place nonpolar, water-fearing residues on its surface, and pack its polar, water-loving residues inside. Then it must find a way to stabilize its structure by creating bonds between the hydrophilic residues within its core.

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With this approach, Lu and his colleagues were able to manufacture the designed transmembrane proteins inside bacteria and mammalian cells by using as many as amino acids. The instability index II for Danio rerio and Cyprinus carpio The models presented here can serve as a guide for the allocation of amino acid residues involved in each fold, which is important for further investigations on the molecular mechanism of functions.

The present study was performed for sequence analyses and prediction of 3D structure of RBP from Danio rerio and Cyprinus carpio using the Homology modelling. A series of molecular modelling and computational methods were combined to gain insight into the 3D structure. Further study, investigating the role of other factors in RBP biosynthesis in wet lab is going on in our laboratory, which could add important information to the overall understanding of the fish model.

Formation of vitamin A in freshwater fish. Origin of retinol in freshwater fish. Distribution of retinol and dehydroretinol in freshwater fish. Amino acid substitution matrices from an information theoretic perspective. Goswami UC and Bhattacharya S. Metabolism of cryptoxanthin in freshwater fish.

Biosynthesis of vitamin A2 Dehydroretinol in freshwater Bagrid, Mystus. Occurence of diversed retinoid molecules in freshwater piscian diversity. Berman H, et al. Nucleic Acids Res Metabolism and utilization and utilization of pigment molecules in designing feeds for freshwater ornamental fish and crustaceans.

Protein Structure and Folding

In Emerging trends in Zoology, edited by U. Goswami J and Goswami UC. Carotenoids pigmentation in Polyacanthus fasciatus during spawning period. Gasteiger E, et al. Apweiler R, et al. Shidoji Y and Muto Y. Vitamin A transport in plasma of the non-mammalian vertebrates: Kyte J and Doolittle R.

Occurrence, Functions and Biological Significance of Arginine-Rich Proteins.

A simple method for displaying the hydropathic character of a protein. Assessment of protein models with three-dimensional profiles. Higgins D, et al. Hooft RWW, et al. Errors in protein structures. Murzin AG, et al. Zemla A, et al. Comparative protein structure prediction. Current Protocols in Protein Science.

Scientists create complex transmembrane proteins from scratch | Newsroom

Fiser A and Sali A. Peicheng Du, et al. Have we seen all structures corresponding to short protein fragments in the Protein Data Bank? An update, Protein Engineering ; Rahman MA, et al. Altschul SF, et al. Improved Tools for Biological Sequence Comparison. Searching protein sequence libraries: Lassmann T and Sonnhammer EL. Automatic assessment of alignment quality.

Fiser A, et al. Modelling of loops in protein structures, Protein Science. Marti-Renom MA, et al.

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Comparative protein structure modelling of genes and genomes. Lassmann T and Erik LL. Sonnhammer Kalign, Kalignvu and Mumsa: Sali A and Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. Giorgetti A, et al. Evaluating the usefulness of protein structure models for molecular replacement. Colovos C and Yeates TO. Verification of protein structures: