Protein-polymer linkages

Protein Polymer and molecular weight Degree of amino group substitution and linkage method Stage in Clinical Trials Ref. 

On the contrary, for reversible protein/polymer complexes, it was important to investigate how salt linkages and hydrophobic association, which... 

Gais, H.J., Rupert, S., Modification and immobilization of proteins with polyethylene glycol tresylates and polysaccharide tresylates evidence suggesting a revision of the coupling mechanism and structure of the polymer-polymer linkage. Tetrahedron Lett. 36, 3837-3838, 1995. 

The building blocks of proteins are the u-amino acids, which are classified as polar or nonpolar, depending on whether the side chain (R group) attached to the a-carbon is hydrophilic or hydrophobic. A protein polymer is built by successive condensation reactions that produce peptide linkages ... 

The nucleophilic terminal amino function of the protein (i.e., the first amino acid residue or monomer of the protein the rest of the amino acids have their amino functions involved in the polymer linkage or nonnucleo-philic amide linkages) will displace the fluorine atom by means of an addition-elimination mechanism. This occurs with the rate-limiting formation of... 

Chemically, proteins are unbranched polymers of amino acids linked head to tail, from carboxyl group to amino group, through formation of covalent peptide bonds, a type of amide linkage (Figure 5.1). 

Larger polymers are known as proteins. Aside from the amide linkages, the polymer chain is very flexible, giving rise to the possibility of an enormous number of different conformers. It is nothing short of remarkable, therefore, that proteins rapidly fold into a single conformation. Very strong forces must be at work. 

Amino acids, the building blocks of giant protein molecules have a carboxyl group and an amino group attached to the same carbon atom. A protein is a linear polymer of amino acids combined by pepfide linkages. Twenfy different amino acids are common in proteins. Their side chains, which have a variety of chemical properties, control the shapes and functions of proteins. Some of these side chains are hydrophobic, others are hydrophilic, and still others occur either on the surface or the interiors of proteins. 

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