In Pre-Sterol Carrier Protein 2 (SCP2) in Solution the Leader Peptide 1-20 is Flexibly Disordered, and Residues 21-143 Adopt the Same Globular Fold As in Mature SCP2
Document Type
Article
Publication Date
8-28-1998
Abstract
The preform of the rabbit sterol carrier protein 2 (pre-rSCP2) was cloned, the uniformly 15N-labelled protein expressed in Escherichia coli and studied by three-dimensional 15N-resolved nuclear magnetic resonance spectroscopy. In spite of its low solubility in aqueous solution of only ~ 0.3 mM, sequential 15N and 1H backbone resonance assignments were obtained for 105 out of the 143 residues. From comparison of the sequential and medium-range nuclear Overhauser effects (NOEs) in the two proteins, all regular secondary structures previously determined in mature human SCP2 (hSCP2) were also identified in pre-rSCP2. Near-identity of the backbone 15N and 1H chemical shifts and 1:1 correspondence of 24 long-range NOEs to backbone amide groups in the two proteins show that the residues 21-143 adopt the same globular fold in pre-rSCP2 and mature hSCP2. The N-terminal 20-residue leader peptide of pre-rSCP2 is flexibly disordered in solution and does not observably affect the conformation of the polypeptide segment 21-143.
DOI
10.1007/s000180050203
Montclair State University Digital Commons Citation
Weber, Franz E.; Dyer, Jim; López García, Francisco; Werder, Moritz; Szyperski, Thomas; Wüthrich, Kurt; and Hauser, Helmut, "In Pre-Sterol Carrier Protein 2 (SCP2) in Solution the Leader Peptide 1-20 is Flexibly Disordered, and Residues 21-143 Adopt the Same Globular Fold As in Mature SCP2" (1998). Department of Chemistry and Biochemistry Faculty Scholarship and Creative Works. 371.
https://digitalcommons.montclair.edu/chem-biochem-facpubs/371