* Protein splicing

Protein splicing is an intramolecular reaction of a particular protein in which an internal protein segment ( called an intein ) is removed from a precursor protein with a ligation of C-terminal and N-terminal external proteins ( called exteins ) on both sides.

Protein splicing was reported by two groups ( Anraku and Stevens ) in 1990.

* Protein splicing mechanism and intein structure

* Protein splicing

* Protein variant forms produced by natural genetic variation, RNA editing, alternative splicing, proteolytic processing, and post-translational modification

Protein is lacking in their natural diet, and should be not be fed in captivity.

Protein biosynthesis is the process in which cells build or manufacture proteins.

Protein folding is the process by which a protein structure assumes its functional shape or conformation.

Protein folding is a very finely tuned process.

Protein adsorption is a process that has a fundamental role in the field of biomaterials.

Protein catabolism, which is the breakdown of macromolecules, is essentially a digestion process.

Protein engineering is the process of developing useful or valuable proteins.

The phosphorylation events lead to a decrease in intracelluar calcium ( inhibit L type Calcium channels, inhibits IP3 receptor channels, stimulates sarcoplasmic reticulum Calcium pump ATPase ), a decrease in the 20kd myosin light chain phosphorylation by altering calcium sensitization and increasing myosin light chain phosphatase activity, a stimulation of calcium sensitive potassium channels which hyperpolarize the cell, and the phosphorylation of amino acid residue serine 16 on the small heat shock protein ( hsp20 ) by Protein Kinases A and G. The phosphorylation of hsp20 appears to alter actin and focal adhesion dynamics and actin-myosin interaction, and recent evidence indicates that hsp20 binding to 14-3-3 protein is involved in this process.

The generally accepted method of purification of process streams for monoclonal antibodies includes capture of the product target with Protein A, elution, acidification to inactivate potential Mammalian viruses, followed by cation exchange chromatography, and finally anion exchange chromatography.

** Protein folding, the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure

The process of osteocytogenesis is largely unknown, but the following molecules have been shown to play a crucial role in the production of healthy osteocytes, either in correct numbers or specific distributions: Matrix Metalloproteinases ( MMPs ), Dentin Matrix Protein 1 ( DMP-1 ), Osteoblast / Osteocyte factor 45 ( OF45 ), Klotho gene, TGF Beta inducile factor ( TIEG ), Lysophosphatidic acid ( LPA ), E11 antigen, and Oxygen.

Protein skimmers use the foam fractionation process wherein air is introduced into a water stream creating microbubbles.

* Protein translocation or protein targeting, a process in protein biosynthesis

Protein H is a multifunctional structural protein required for piloting the viral DNA into the host cell interior during the entry process.

Members of the subfamily Microvirinae have four structural proteins: major capsid protein F, major spike protein G, a small DNA-binding protein J ( 25-40 amino acids in length ) and DNA pilot protein H. Assembly of the viron uses two scaffolding proteins, internal scaffolding protein B and external scaffolding protein D. Protein H is a multifunctional structural protein required for piloting the viral DNA into the host cell interior during the entry process.

For example, synthetic peptides can be used as probes to see where protein-peptide interactions occur-see the page on Protein tags.

Protein cores made in the rough endoplasmic reticulum are posttranslationally modified by glycosyltransferases in the Golgi apparatus, where GAG disaccharides are added to protein cores to yield proteoglycans ; the exception is the GAG hyaluronan, which is uniquely synthesized without a protein core and is " spun out " by enzymes at the cell surface directly into the extracellular space.

One type of AAA Proteins are AAA Proteases, where the energy from ATP hydrolysis is used to translocate a Protein inside the Protease for degradation.

From 1994-1997 Nölting was scientist at Cambridge University and the Cambridge Centre for Protein Engineering ( UK ) where he developed, together with Sir Alan R. Fersht, methods for the high resolution of protein folding.

The best characterized function of Protein S is its role in the anti coagulation pathway, where it functions as a cofactor to Protein C in the inactivation of Factors Va and VIIIa.

This flesh would then be contributed to the ' Protein Bank ', where it would be used to feed either the Lexx or the Gigashadow, or used in the creation of cyborgs.

Protein subcellular localization prediction involves the computational prediction of where a protein resides in a cell.

Protein A, protein G, and protein L are examples of proteins that strongly bind to various antibody isotypes.

Protein sequence can be determined by Edman degradation, in which the N-terminal residues are hydrolyzed from the chain one at a time, derivatized, and then identified.

Low carbohydrate diets such as Atkins and Protein Power are relatively high in protein and fats.

Protein crystals are formed in salt solutions.

Solved structures are usually deposited in the Protein Data Bank ( PDB ), a freely available resource from which structural data about thousands of proteins can be obtained in the form of Cartesian coordinates for each atom in the protein.

Protein kinases are also found in bacteria and plants.

The images below are of Lipscomb's structures from the Protein Data Bank displayed in simplified form with atomic detail suppressed.

C: Microdialysis Protein crystals are almost always grown in solution.

Three-dimensional protein structures of the peroxidated catalase intermediates are available at the Protein Data Bank.

Some of the more recognized diets are Bourbon's Modified Leadbeaters ( BML ), High Protein Wombaroo ( HPW ), various calcium rich diets and Leadbeaters Mixture ( LBM ).

Protein formation and destruction are both accelerated in hyperthyroidism.

Protein kinases are a group of enzymes that possess a catalytic subunit that transfers the gamma ( terminal ) phosphate from nucleotide triphosphates ( often ATP ) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function.

There are over 100 3D structures of tyrosine kinases available at the Protein Data Bank.

Approximately 2000 kinases are known, and more than 90 Protein Tyrosine Kinases ( PTKs ) have been found in the human genome.

Protein tyrosine kinases that are encoded by the Rous sarcoma virus cause cellular transformation, and are termed oncoproteins.

Transpeptidases, such as the sortases responsible for anchoring factors like Protein A to the staphylococcal peptidoglycan, are being studied in hopes of developing new antibiotics to target MRSA infections.

Protein sequences are frequently aligned using substitution matrices that reflect the probabilities of given character-to-character substitutions.

In addition, structures of many water-soluble domains of IMPs are available in the Protein Data Bank.

Protein expression systems are very widely used in the life sciences, biotechnology and medicine.

Protein expression systems are used to produce certain proteins in biotechnology and industry, and more recently to produce sets ( combinatorial series ) of protein that are screened for drug discovery purpose.

Protein levels are evaluated through densitometry ( how intense the stain is ) or spectrophotometry.

Protein molecules — either of the host's own phenotype or of other biologic entities — are continually synthesized and degraded in a cell.