Proteins are made of amino acid chains, or polypeptides. Amino acids have a basic backbone made of an amino group and a carboxyl group, and differ in their side-chains. These polypeptide chains of ...

In the protein's final, or native, three-dimensional conformation, also known as its tertiary structure, some of these thiol groups are oxidized to form disulfide bonds. Reduction of these bonds ...

β-pleated sheet: N-H groups in the backbone of one strand form hydrogen bonds with ... the folding of the proteins and, hence, its function in the body. The tertiary structure of proteins refers ...

which are linked together by peptide bonds and folded into specific three-dimensional structures. Proteins have four levels of structure: primary (amino acid sequence), secondary (local folding ...

FVIII, the blood clotting protein missing in hemophilia A, adopts multiple shapes, making it more likely to be targeted by ...

Our overall hydrogen bond patterns could be used to annotate protein secondary and tertiary structure, which may lead to a valuable and robust new classification of protein folds 11,20.

A major limitation with the existing PEGylated proteins is their heterogeneous nature. This is because PEG is conjugated at many different nucleophilic amine residues in the protein 4,5,6.

Raman spectroscopy enables monitoring of the changes in secondary and tertiary protein structure. The combination of DLS and Raman spectroscopy allows measurement of protein size and structure from a ...

Raman spectroscopy enables monitoring of the changes in secondary and tertiary protein structure. The combination of DLS and Raman spectroscopy allows measurement of protein size and structure from a ...