title: Ð¤Ð¾Ð»Ð´Ð¸Ð½Ð³ Ð±ÑÑÑÐµÐ³Ð¾ Ð¾Ð´Ð¾ÑÐ°Ð½Ñ-ÑÐ²ÑÐ·ÑÐ²Ð°ÑÑÐµÐ³Ð¾ Ð±ÐµÐ»ÐºÐ° Ð² ÑÐ°ÑÑÐ²Ð¾ÑÐµ Ð¸ Ð² ÑÑÐ»Ð¾Ð²Ð¸ÑÑ ÐºÑÐ°ÑÐ´Ð¸Ð½Ð³Ð°
title: Ð±Ð°ÐºÐ°Ð»Ð°Ð²ÑÑÐºÐ°Ñ ÑÐ°Ð±Ð¾ÑÐ°
titleType: Subtitle
Creators: name: Ð Ð¾Ð³Ð¸Ð½ÑÐºÐ¸Ð¹, ÐÐµÐ½Ð¸Ñ
Publisher: name: Ð¡Ð°Ð½ÐºÑ-ÐÐµÑÐµÑÐ±ÑÑÐ³ÑÐºÐ¸Ð¹ Ð¿Ð¾Ð»Ð¸ÑÐµÑÐ½Ð¸ÑÐµÑÐºÐ¸Ð¹ ÑÐ½Ð¸Ð²ÐµÑÑÐ¸ÑÐµÑ ÐÐµÑÑÐ° ÐÐµÐ»Ð¸ÐºÐ¾Ð³Ð¾
Year: 2016
Subjects: ÑÐ¾Ð»Ð´Ð¸Ð½Ð³ Ð±ÐµÐ»ÐºÐ¾Ð²
Ð¾Ð´Ð¾ÑÐ°Ð½Ñ-ÑÐ²ÑÐ·ÑÐ²Ð°ÑÑÐ¸Ðµ Ð±ÐµÐ»ÐºÐ¸
Ð¾Ð±Ð¼ÐµÐ½ Ð´Ð¾Ð¼ÐµÐ½Ð°Ð¼Ð¸
Ð´ÐµÐ½Ð°ÑÑÑÐ°ÑÐ¸Ñ
Ð¼Ð¾Ð»ÐµÐºÑÐ»ÑÑÐ½ÑÐ¹ ÐºÑÐ°ÑÐ´Ð¸Ð½Ð³
odorant-binding protein
domain swapping
protein folding
denaturation
molecular crowding

description: Ð¦ÐµÐ»ÑÑ ÑÐ°Ð±Ð¾ÑÑ ÑÐ²Ð»ÑÐµÑÑÑ Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ðµ Ð²Ð»Ð¸ÑÐ½Ð¸Ñ Ð¾Ð±ÑÐ°Ð·Ð¾Ð²Ð°Ð½Ð¸Ñ ÐºÐ¾Ð¼Ð¿Ð»ÐµÐºÑÐ° Ñ Ð¿ÑÐ¸ÑÐ¾Ð´Ð½ÑÐ¼ Ð»Ð¸Ð³Ð°Ð½Ð´Ð¾Ð¼ 1-Ð¾ÐºÑÐµÐ½-3-Ð¾Ð»Ð¾Ð¼ Ð¸ ÑÑÐ»Ð¾Ð²Ð¸Ð¹ Ð¼Ð°ÐºÑÐ¾Ð¼Ð¾Ð»ÐµÐºÑÐ»ÑÑÐ½Ð¾Ð³Ð¾ ÐºÑÐ°ÑÐ´Ð¸Ð½Ð³Ð° Ð½Ð° ÑÑÑÑÐºÑÑÑÑ, ÑÑÐ°Ð±Ð¸Ð»ÑÐ½Ð¾ÑÑÑ Ð¸ Ð¿ÑÐ¾ÑÐµÑÑÑ ÑÐ¾Ð»Ð´Ð¸Ð½Ð³Ð° ÑÐµÐºÐ¾Ð¼Ð±Ð¸Ð½Ð°Ð½ÑÐ½Ð¾Ð³Ð¾ Ð±ÑÑÑÐµÐ³Ð¾ Ð¾Ð´Ð¾ÑÐ°Ð½Ñ-ÑÐ²ÑÐ·ÑÐ²Ð°ÑÑÐµÐ³Ð¾ Ð±ÐµÐ»ÐºÐ° (bOBP), Ð° ÑÐ°ÐºÐ¶Ðµ ÑÐ¾Ð»Ð¸ Ð¼ÐµÑÐ°Ð½Ð¸Ð·Ð¼Ð° Â«Ð¾Ð±Ð¼ÐµÐ½Ð° Ð´Ð¾Ð¼ÐµÐ½Ð¾Ð²Â» Ð² Ð¿Ð¾Ð´Ð´ÐµÑÐ¶Ð°Ð½Ð¸Ð¸ Ð½Ð°ÑÐ¸Ð²Ð½Ð¾Ð¹ ÑÑÑÑÐºÑÑÑÑ Ð±ÐµÐ»ÐºÐ° Ð¸ Ð¿ÑÐ¾ÑÐµÑÑÐ°Ñ ÐµÐ³Ð¾ ÑÐ¾Ð»Ð´Ð¸Ð½Ð³Ð°. ÐÐ¾ÐºÐ°Ð·Ð°Ð½Ð¾, ÑÑÐ¾ Ð²ÑÑÐ°Ð²ÐºÐ° Ð³Ð»Ð¸ÑÐ¸Ð½Ð° Ð¿Ð¾ÑÐ»Ðµ Ð°Ð¼Ð¸Ð½Ð¾ÐºÐ¸ÑÐ»Ð¾ÑÐ½Ð¾Ð³Ð¾ Ð¾ÑÑÐ°ÑÐºÐ° 121 Ð¿ÑÐ¸Ð²Ð¾Ð´Ð¸Ñ Ðº Ð¾Ð±ÑÐ°Ð·Ð¾Ð²Ð°Ð½Ð¸Ñ ÑÑÐ°Ð±Ð¸Ð»ÑÐ½Ð¾Ð¹ Ð¼Ð¾Ð½Ð¾Ð¼ÐµÑÐ½Ð¾Ð¹ Ð¼ÑÑÐ°Ð½ÑÐ½Ð¾Ð¹ ÑÐ¾ÑÐ¼Ñ. ÐÐµÑÐ°Ð½Ð¸Ð·Ð¼ Â«Ð¾Ð±Ð¼ÐµÐ½Ð° Ð´Ð¾Ð¼ÐµÐ½Ð¾Ð²Â» Ð½Ðµ Ð¿ÑÐ¸Ð²Ð¾Ð´Ð¸Ñ Ðº ÑÑÑÐµÑÑÐ²ÐµÐ½Ð½Ð¾Ð¹ ÑÑÐ°Ð±Ð¸Ð»Ð¸Ð·Ð°ÑÐ¸Ð¸ ÑÑÑÑÐºÑÑÑÑ Ð±ÐµÐ»ÐºÐ°, ÑÐ¾Ð³Ð´Ð° ÐºÐ°Ðº Ð²Ð²ÐµÐ´ÐµÐ½Ð¸Ðµ ÐºÐ°Ð½Ð¾Ð½Ð¸ÑÐµÑÐºÐ¾Ð¹ Ð´Ð¸ÑÑÐ»ÑÑÐ¸Ð´Ð½Ð¾Ð¹ ÑÐ²ÑÐ·Ð¸ Ð½Ð°Ð¿ÑÐ¾ÑÐ¸Ð² ÑÑÐ°Ð±Ð¸Ð»Ð¸Ð·Ð¸ÑÑÐµÑ ÑÑÑÑÐºÑÑÑÑ Ð¼Ð¾Ð½Ð¾Ð¼ÐµÑÐ½Ð¾Ð¹ Ð¼ÑÑÐ°Ð½ÑÐ½Ð¾Ð¹ ÑÐ¾ÑÐ¼Ñ. Ð¡Ð²ÑÐ·ÑÐ²Ð°Ð½Ð¸Ðµ Ð»Ð¸Ð³Ð°Ð½Ð´Ð° Ð¿ÑÐ¸Ð²Ð¾Ð´Ð¸Ñ Ðº ÑÑÑÐµÑÑÐ²ÐµÐ½Ð½Ð¾Ð¹ ÑÑÐ°Ð±Ð¸Ð»Ð¸Ð·Ð°ÑÐ¸Ð¸ ÑÑÑÑÐºÑÑÑÑ Ð¸ÑÑÐ»ÐµÐ´ÑÐµÐ¼ÑÑ Ð±ÐµÐ»ÐºÐ¾Ð². ÐÑÐ°ÑÐ´Ð¸Ð½Ð³ Ð°Ð³ÐµÐ½Ñ Ð¿Ð¾Ð»Ð¸ÑÑÐ¸Ð»ÐµÐ½Ð³Ð»Ð¸ÐºÐ¾Ð»Ñ Ð¿ÑÐ¸Ð²Ð¾Ð´Ð¸Ñ Ðº ÑÑÐ°Ð±Ð¸Ð»Ð¸Ð·Ð°ÑÐ¸Ð¸ bOBP Ð¸ ÑÐ¿Ð¾ÑÐ¾Ð±ÑÑÐ²ÑÐµÑ Ð¾Ð±ÑÐ°Ð·Ð¾Ð²Ð°Ð½Ð¸Ñ Ð½Ð°ÑÐ¸Ð²Ð½Ð¾Ð³Ð¾ Ð´Ð¸Ð¼ÐµÑÐ½Ð¾Ð³Ð¾ ÑÐ¾ÑÑÐ¾ÑÐ½Ð¸Ñ Ð±ÐµÐ»ÐºÐ° Ð´Ð°Ð¶Ðµ Ð² Ð¾ÑÑÑÑÑÑÐ²Ð¸Ðµ Ð´ÐµÐ½Ð°ÑÑÑÐ¸ÑÑÑÑÐ¸Ñ ÑÑÐ»Ð¾Ð²Ð¸Ð¹. Ð­ÑÑÐµÐºÑ ÐºÑÐ°ÑÐ´Ð¸Ð½Ð³ Ð°Ð³ÐµÐ½ÑÐ° Ð·Ð°Ð²Ð¸ÑÐ¸Ñ Ð¾Ñ ÐµÐ³Ð¾ Ð¼Ð¾Ð»ÐµÐºÑÐ»ÑÑÐ½Ð¾Ð¹ Ð¼Ð°ÑÑÑ Ð¸ ÐºÐ¾Ð½ÑÐµÐ½ÑÑÐ°ÑÐ¸Ð¸.
description: In this work we investigated the effect of formation of a complex with natural ligand 1-octen-3-ol and molecular crowding milieu on structure, stability and folding of recombinant bovine odorant-binding protein (bOBP). We also investigated a role of Â«domain swappingÂ» in maintaining of the native protein structure and in its folding processes. It was shown that the insertion of glycine after residue 121 prevents Â«domain swappingÂ» and generates stable monomeric protein bOBP/Gly121+. Â«Domain swappingÂ» doesn't contribute much to the conformational stability of a protein. In contrast, introduction of a disulfide bond to the structure of a monomeric protein promotes significant stabilizing effect. Binding of the natural ligand leads to increase of conformational stability of the studied proteins. Crowding agent polyethylene glycol stabilizes bOBP and induces formation of the native dimeric state, even in the absence of denaturant. The effect of crowding agents depends on its molecular mass and concentration.