Avtor/Urednik		Stopar, David; Hemminga, Marcus A
Naslov		Lokacija in struktura glavnega plaščnega proteina bakteriofaga M13 med razstavljanjem in sestavljanjem virusa
Tip		članek
Vir		In: Bole-Hribovšek V, Ocepek M, Klun N, editors. Zbornik s programom 2. kongres slovenskih mikrobiologov z mednarodno udeležbo; 1998 sep 27-30; Portorož. Ljubljana: Slovensko mikrobiološko društvo,
Leto izdaje		1998
Obseg		str. 398-400
Jezik		slo
Abstrakt		Mutants of the M13 bacteriophage major coat protein containing single cysteine replacements in the hydrophobic and C-terminal domain were purified from viable phage. These were used for site-directed spin-labeling to determine the location and assembly of the major coat protein incorporated in bilayer membranes of dioleoylphosphatidilcholine. The membrane location of the spin-labeled cysteine residue was studied with molecular oxygen and Ni2+ ions as paramagnetic relaxation agents preferentially confined to the hydrophobic and aqueous regions, respectively, by using progressive saturation electron spin resonance spectroscopy. The section of the protein around Thr36 is situated at the center of the membrane. Residue Thr46 is placed at the membrane surface in the phospholipide headgroup region which leaves a short C-terminal section in the aqueous phase. Residue Ala25 is then consistently placed in the head group region of the opposing lipid monolayer leaflet. Such a topology of the protein enables C-terminal positive charges, which are important in protein: DNA interastions, to be protected in the lipid head group, and the protein can be assembled in the new virus particle only when lipids are removed at the assembly site.