[Conformational status of apomyoglobin in the presence of phospholipid vesicles at neutral pH].
The conformational state of sperm whale apomyoglobin (apoMb) was studied at neutral pH in the presence of negatively charged vesicles using near- and far-UV circular dichroism, tryptophan fluorescence, differential scanning microcalorimetry, and fast performance liquid chromatography. Under these conditions, the apoMb structure undergoes transition from its native to an intermediate state. In this state the protein loses its rigid native structure but retains its secondary structure. However, the environment of tryptophan residues remains rather hydrophobic. This intermediate state of apoMb shows properties similar to those of its molten globule state in solution. It is shown that apoMb can bind to negatively charged phospholipid vesicles even at neutral pH. A possible functional role of this intermediate state is discussed.
Basov
L V
LV
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia. liana@vega.protres.ru
Tiktopulo
E I
EI
Kashparov
I A
IA
Bychkova
V E
VE
D001059:Apoproteins / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D006863:Hydrogen-Ion Concentration; D009211:Myoglobin / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet
D001059:Apoproteins; D009211:Myoglobin; D010743:Phospholipids; C010857:apomyoglobin