Thermodynamic analysis of human plasma apolipoprotein C-1: high-temperature unfolding and low-temperature oligomer dissociation.


Abstract

Thermal and chemical unfolding of lipid-free apolipoprotein C-1 (apoC-1), a 6-kDa protein component of very low density and high-density lipoproteins, was analyzed by far-UV CD. In neutral 1 mM Na2HPO4 solutions containing 6-7 micrograms/mL protein, the apoC-1 monomer is approximately 30% alpha-helical at 0-22 degrees C and unfolds reversibly from about 22-80 degrees C with Tm = 51 +/- 3 degrees C and van't Hoff enthalpy delta Hv(Tm) = 19 +/- 3 kcal/mol. The apparent free energy of the monomer stabilization determined from the chemical unfolding at 0 degree C, delta G(0 degree C) = 2.8 +/- 0.8 kcal/mol, decreases by about 1 kcal/mol upon heating to 25 degrees C. A small apparent heat capacity increment suggests the absence of a substantial hydrophobic core for the apoC-1 molecule. At pH 7, increasing apoC-1 concentration above 10 micrograms/mL leads to self-association and formation of additional alpha-helices that unfold upon both heating and cooling from room temperature. The CD data indicate that the high-temperature transition reflects a complete monomer unfolding and the low-temperature transition reflects oligomer dissociation into stable monomers. This suggests the importance of hydrophobic interactions for apoC-1 self-association. Close proximity between the high- and low-temperature transitions and the absence of a plateau in the chemical unfolding curves recorded from oligomeric apoC-1 indicate marginal oligomer stability and suggest that in vivo apoC-1 transfer is mediated via the complexes with other apolipoproteins and/or lipids. Study holds ProTherm entries: 17824, 17825, 17826 Extra Details: Monomer apolipoprotein C-1, hydrophobic interaction, high temperature unfolding, oligomer dissociation.

Submission Details

ID: bvAE8Qaz3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:50 p.m.

Version: 1

Publication Details
Gursky O;Atkinson D,Biochemistry (1998) Thermodynamic analysis of human plasma apolipoprotein C-1: high-temperature unfolding and low-temperature oligomer dissociation. PMID:9477954
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1OPP 1998-05-13 PEPTIDE OF HUMAN APOLIPOPROTEIN C-I RESIDUES 1-38, NMR, 28 STRUCTURES
1IOJ 1998-08-12 HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES
1ALE 1995-04-20 CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY
1ALF 1995-04-20 CONFORMATION OF TWO PEPTIDES CORRESPONDING TO HUMAN APOLIPOPROTEIN C-I RESIDUES 7-24 AND 35-53 IN THE PRESENCE OF SODIUM DODECYLSULFATE BY CD AND NMR SPECTROSCOPY
6DVU 2018-12-26 1.8 Structure of the Monoclinic-1 (Monocl-1) Crystal Form of Human Apolipoprotein C1
6DXR 2018-12-26 2.0 Structure of the Monoclinic-2 (Monocl-2) Crystal Form of Human Apolipoprotein C1
6NF3 2018-12-26 2.33 Structure of the Monoclinic-3 (Monocln-3) Crystal Form of Human Apolipoprotein C1
6DZ6 2018-12-26 3.0 Structure of the Orthorhombic (Orthrhmb) Crystal Form of Human Apolipoprotein C1

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
92.3 Apolipoprotein C-I P0CE40 APO1B_PONAB
98.8 Apolipoprotein C-I P0CE38 APO1B_PANTR
100.0 Apolipoprotein C-I P02654 APOC1_HUMAN