What is the function of quaternary protein structure?

Quaternary structure is an important protein attribute that is closely related to its function. Proteins with quaternary structure are called oligomeric proteins. Oligomeric proteins are involved in various biological processes, such as metabolism, signal transduction, and chromosome replication.

Who discovered Ramachandran plot?

Gopalasamudram Narayanan Ramachandran
Gopalasamudram Narayanan Ramachandran, or G.N. Ramachandran, FRS (8 October 1922 – 7 April 2001) was an Indian physicist who was known for his work that led to his creation of the Ramachandran plot for understanding peptide structure. He was the first to propose a triple-helical model for the structure of collagen.

What is the function of secondary protein structure?

Secondary structure of the proteins can be used to predict the tertiary structure since predicting only with amino acid sequence may not be sufficient. The secondary structure of proteins is determined by the pattern of hydrogen bonding.

What do Ramachandran plots show quizlet?

Ramachandran plots describe the combinations of Φ and Ψ dihedral angles that are or are not permitted in a peptide backbone.

What forces hold quaternary structure together?

The quaternary structure of a protein is the association of several protein chains or subunits into a closely packed arrangement. Each of the subunits has its own primary, secondary, and tertiary structure. The subunits are held together by hydrogen bonds and van der Waals forces between nonpolar side chains.

What best describes the quaternary structure of protein?

Explanation: Quaternary structure describes how polypeptide chains fit together to form a complete protein. Quaternary protein structure is held together by hydrophobic interactions, and disulfide bridges. “The four parts of a protein’s amino acid sequence” does not refer to anything in particular.

What is Ramachandran plot PPT?

The Ramachandran Plot • The two torsion angles of the polypeptide chain, describe the rotations of the polypeptide backbone around the bonds between N-Cα (called Phi, φ) and Cα-C (called Psi, ψ) • It provides an easy way to view the distribution of torsion angles of a protein structure.

Is secondary structure of protein functional?

Protein structure plays a key role in its function; if a protein loses its shape at any structural level, it may no longer be functional. Secondary structure is local interactions between stretches of a polypeptide chain and includes α-helix and β-pleated sheet structures.

Why does glycine have a unique Ramachandran plot?

Regions in the glycine Ramachandran plot. Glycine is fundamentally different to the other amino acids in that it lacks a sidechain. In particular, glycine does not have the Cβ atom, which induces many steric clashes in the generic Ramachandran plot.

Who is the creator of the Ramachandran plot?

In biochemistry, a Ramachandran plot (also known as a Rama plot, a Ramachandran diagram or a [φ,ψ] plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V. Sasisekharan, is a way to visualize energetically allowed regions for backbone dihedral angles ψ against φ of amino acid residues in protein structure.

What are the regions of the Ramachandran plot?

A Ramachandran plot generated from human PCNA, a trimeric DNA clamp protein that contains both β-sheet and α-helix (PDB ID 1AXC). The red, brown, and yellow regions represent the favored, allowed, and “generously allowed” regions as defined by ProCheck.

How is the Ramachandran plot different from the proline plot?

In contrast, the Ramachandran plot for proline, with its 5-membered-ring side chain connecting Cα to backbone N, shows a limited number of possible combinations of ψ and φ (see Pro plot in gallery ). The residue preceding proline (“pre-proline”) also has limited combinations compared to the general case.