What is the primary driving force for the folding of most soluble, globular proteins?
Explanation
The folding of soluble proteins is primarily driven by the hydrophobic effect. The clustering of nonpolar side chains in the protein's interior minimizes the ordering of water molecules around them, leading to a favorable increase in the entropy of the solvent, which is the major thermodynamic driving force.
Other questions
According to the convention for dihedral angles in a peptide backbone, what values are assigned to phi and psi when the polypeptide is in its fully extended conformation?
What are the characteristic number of residues per turn and the rise along the helical axis for an idealized alpha-helix?
Which amino acid residue introduces a destabilizing kink in an alpha-helix and is thus only rarely found within one?
In the Anfinsen experiment, what was the significance of the observation that denatured and reduced ribonuclease A could spontaneously refold into its native, catalytically active form?
What is the structural basis for the strength of silk fibroin?
A polypeptide with 80 amino acid residues is in a single contiguous alpha-helix. What is the approximate length of this helix?
What is the term for a recognizable folding pattern involving two or more elements of secondary structure and their connection, such as a beta-alpha-beta loop?
What is the primary characteristic of intrinsically disordered proteins?
Which protein is composed of a triple helix of polypeptide chains, with a repeating Gly-X-Y sequence?
In a Ramachandran plot, what do the shaded regions represent?
What is the term for a disease, such as Alzheimer disease, that is associated with the conversion of a normally soluble protein into an insoluble extracellular amyloid fiber?
In the structure of myoglobin, where are the majority of the hydrophobic R groups located?
Which technique is used to assess the secondary structure of proteins by measuring the difference in absorption of left-handed versus right-handed circularly polarized light?
What is the typical rise per residue along the central axis of an idealized alpha-helix?
What distinguishes parallel from antiparallel beta-sheets?
The protein that makes up hair and wool, alpha-keratin, is an example of which type of protein?
Levinthal's paradox addresses the problem of:
Which of the following describes the quaternary structure of a protein?
What type of enzyme catalyzes the interchange of disulfide bonds to facilitate correct protein folding?