what is the name of the kinetic intermediate in protein folding where secondary structure elements have formed their regular H-bonding patterns and there has been collapse to separate most nonpolar side chains into the protein interior and most hydrophilic side chains to the protein exterior, but the side chain packing has not yet been optimized to achieve a tightly packed protein interior with a crystalline density?
Cite this post:
Sourav Pan. (2025, April 23). what is the name of the kinetic intermediate in protein folding where secondary structure elements have formed their regular H-bonding patterns and there has been collapse to separate most nonpolar side chains into the protein interior and most hydrophilic side chains to the protein exterior, but the side chain packing has not yet been optimized to achieve a tightly packed protein interior with a crystalline density?. Biology Notes Online. Retrieved from https://biologynotesonline.com/qa/what-is-the-name-of-the-kinetic-intermediate-in-protein-folding-where-secondary-structure-elements-have-formed-their-regular-h-bonding-patterns-and-there-has-been-collapse-to-separate-most-nonpolar-si/
Sourav Pan. "what is the name of the kinetic intermediate in protein folding where secondary structure elements have formed their regular H-bonding patterns and there has been collapse to separate most nonpolar side chains into the protein interior and most hydrophilic side chains to the protein exterior, but the side chain packing has not yet been optimized to achieve a tightly packed protein interior with a crystalline density?." Biology Notes Online, 23 April 2025, biologynotesonline.com/qa/what-is-the-name-of-the-kinetic-intermediate-in-protein-folding-where-secondary-structure-elements-have-formed-their-regular-h-bonding-patterns-and-there-has-been-collapse-to-separate-most-nonpolar-si/.
Sourav Pan. "what is the name of the kinetic intermediate in protein folding where secondary structure elements have formed their regular H-bonding patterns and there has been collapse to separate most nonpolar side chains into the protein interior and most hydrophilic side chains to the protein exterior, but the side chain packing has not yet been optimized to achieve a tightly packed protein interior with a crystalline density?." Biology Notes Online (blog). April 23, 2025. https://biologynotesonline.com/qa/what-is-the-name-of-the-kinetic-intermediate-in-protein-folding-where-secondary-structure-elements-have-formed-their-regular-h-bonding-patterns-and-there-has-been-collapse-to-separate-most-nonpolar-si/.
The kinetic intermediate in protein folding characterized by the formation of regular hydrogen-bonded secondary structures and the segregation of nonpolar side chains into the protein interior, while lacking optimized side chain packing, is termed the “molten globule” state.
This intermediate exhibits native-like secondary structure and a compact overall shape but lacks the specific tight packing of amino acid residues that defines the fully folded native state.
The molten globule state is a common feature in the folding pathways of many globular proteins, representing a partially folded conformation that precedes the attainment of the native structure.
Understanding the molten globule state is crucial for elucidating the mechanisms of protein folding and misfolding, with implications for various biological processes and diseases.
Cite this post:
Sourav Pan. (2025, April 23). what is the name of the kinetic intermediate in protein folding where secondary structure elements have formed their regular H-bonding patterns and there has been collapse to separate most nonpolar side chains into the protein interior and most hydrophilic side chains to the protein exterior, but the side chain packing has not yet been optimized to achieve a tightly packed protein interior with a crystalline density?. Biology Notes Online. Retrieved from https://biologynotesonline.com/qa/what-is-the-name-of-the-kinetic-intermediate-in-protein-folding-where-secondary-structure-elements-have-formed-their-regular-h-bonding-patterns-and-there-has-been-collapse-to-separate-most-nonpolar-si/
Sourav Pan. "what is the name of the kinetic intermediate in protein folding where secondary structure elements have formed their regular H-bonding patterns and there has been collapse to separate most nonpolar side chains into the protein interior and most hydrophilic side chains to the protein exterior, but the side chain packing has not yet been optimized to achieve a tightly packed protein interior with a crystalline density?." Biology Notes Online, 23 April 2025, biologynotesonline.com/qa/what-is-the-name-of-the-kinetic-intermediate-in-protein-folding-where-secondary-structure-elements-have-formed-their-regular-h-bonding-patterns-and-there-has-been-collapse-to-separate-most-nonpolar-si/.
Sourav Pan. "what is the name of the kinetic intermediate in protein folding where secondary structure elements have formed their regular H-bonding patterns and there has been collapse to separate most nonpolar side chains into the protein interior and most hydrophilic side chains to the protein exterior, but the side chain packing has not yet been optimized to achieve a tightly packed protein interior with a crystalline density?." Biology Notes Online (blog). April 23, 2025. https://biologynotesonline.com/qa/what-is-the-name-of-the-kinetic-intermediate-in-protein-folding-where-secondary-structure-elements-have-formed-their-regular-h-bonding-patterns-and-there-has-been-collapse-to-separate-most-nonpolar-si/.
