A Protein Dissection Study of a Molten Globule

Biochemistry. 1994 Mar 1;33(8):2136-41. doi: 10.1021/bi00174a021.

Abstract

Proteins have many distinct tertiary folds (Richardson, J. S. (1981) Adv. Prot. Chem. 34, 167-339). The term tertiary fold refers to the spatial organization of secondary structure elements (alpha-helices and beta-strands). It is not known when, in the process of protein folding, a native tertiary fold emerges. Here, we show that the helical domain of human alpha-lactalbumin, in isolation, forms a molten globule with the same overall tertiary fold as that found in intact alpha-lactalbumin. Formation of this native-like fold does not require extensive, specific side-chain packing. Our results suggest that much of the information transfer from one-dimension to three-dimensions has occurred at the molten globule stage of protein folding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Circular Dichroism
  • Humans
  • Lactalbumin / chemistry*
  • Light
  • Magnetic Resonance Spectroscopy
  • Protein Folding
  • Scattering, Radiation
  • Spectrophotometry, Ultraviolet

Substances

  • Lactalbumin