tertiary fold

Protein binding to helical junctions is important for initiating the correct tertiary fold of RNA and to organize the overall structure.

Amyloid beta is commonly thought to be intrinsically unstructured, meaning that in solution it does not acquire a unique tertiary fold but rather populates a set of structures.

One of the most intriguing features among members of this class of proteins is although they all exhibit the same tertiary fold there is very little sequence similarity between them.

The network consisted of both residues spatially close to the binding site in the tertiary fold, called contact pairs, and more distant residues that participate in longer-range energetic interactions.

The crystal structure of PTX3 has not been determined yet, however according to modeling, the PTX3 pentraxin domain well-accommodates on the tertiary fold of SAP, with almost all of the β-strands and the α-helical segments conserved.

Tetraloop-receptor interactions combine base-pairing and stacking interactions between the loop nucleotides of a tetraloop motif and a receptor motif located within an RNA duplex, creating a tertiary contact that stabilizes the global tertiary fold of an RNA molecule.

In 1995, James H. Prestegard and coworkers demonstrated that NMR spectra of certain proteins (in this case cyanometmyoglobin, which has a very highly anisotropic paramagnetic susceptibility), taken at very high field, may contain data that can usefully complement NOEs in determining a tertiary fold.

When examining the gel produced by running the gels on a band the areas of various strength of protection where areas of stronger protection for hydroxyl radicals can be said to have tighter association with a protein, or if no protein associates with the nucleic acid it can be caused by the tertiary fold.