protein tertiary structure

Protein tertiary structure can be divided into four main classes based on the secondary structural content of the domain.

Within biophysics, he is known for experiment and theory in understanding the dynamical behavior of protein tertiary structure.

Protein tertiary structure - arrangement of the protein atoms in three dimensional space.

This process is usually applied to protein tertiary structures but can also be used for large RNA molecules.

The method of homology modeling is based on the observation that protein tertiary structure is better conserved than amino acid sequence.

Effective prion decontamination relies upon protein hydrolysis or reduction or destruction of protein tertiary structure.

In computational biology, de novo protein structure prediction refers to an algorithmic process by which protein tertiary structure is predicted from its amino acid primary sequence.

Peptide plane flips have been observed in the dynamics of native state protein tertiary structures by comparing crystal structures of the same proteins in multiple conformations.

Like Chou-Fasman, the GOR method is based on probability parameters derived from empirical studies of known protein tertiary structures solved by X-ray crystallography.

MODELLER is a computer program used in producing homology models of protein tertiary structures as well as quaternary structures (rarer).

SEC can also assay protein tertiary structure, as it measures the hydrodynamic volume (not molecular weight), allowing folded and unfolded versions of the same protein to be distinguished.

Perhaps because of this additional need for structural flexibility, lipid anchors are usually bound to the highly flexible segments of proteins tertiary structure that are not well resolved by protein crystallographic studies.

PHYRE2 protein tertiary structure tool suggests that RUFY2 has 15 alpha helices and the longest helix spanning amino acids 199...512 as seen in the figure to the right.

This specialized part of the protein tertiary structure, a positively charged belt in between two hydrophobic (and ionically inert) regions, has been suggested as the trigger for bacterial aggregation influence by the protein.

The Database of protein conformational diversity (PCDB) is a database of diversity of protein tertiary structures within protein domains as determined by X-ray crystallography.

One of the strongest lines of evidence for the supposition that all the relevant information needed to encode protein tertiary structure is found in the primary sequence was demonstrated in the 1950s by Christian Anfinsen.

Upon removal of the protein from this environment, the denatured and functionless ribonuclease protein spontaneously recoiled and regained function, demonstrating that protein tertiary structure is encoded in the primary amino acid sequence.

Predicting protein tertiary structure from only its amino acid sequence is a very challenging problem (see protein structure prediction), but using the simpler secondary structure definitions is more tractable and has been the focus for research for a long time.