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 <front>
  <journal-meta>
   <journal-id journal-id-type="publisher-id">Russian Journal of Biological Physics and Chemisrty</journal-id>
   <journal-title-group>
    <journal-title xml:lang="en">Russian Journal of Biological Physics and Chemisrty</journal-title>
    <trans-title-group xml:lang="ru">
     <trans-title>АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ</trans-title>
    </trans-title-group>
   </journal-title-group>
   <issn publication-format="print">2499-9962</issn>
  </journal-meta>
  <article-meta>
   <article-id pub-id-type="publisher-id">54179</article-id>
   <article-categories>
    <subj-group subj-group-type="toc-heading" xml:lang="ru">
     <subject>МОЛЕКУЛЯРНАЯ БИОФИЗИКА И ФИЗИКА БИОМОЛЕКУЛ</subject>
    </subj-group>
    <subj-group subj-group-type="toc-heading" xml:lang="en">
     <subject>MOLECULAR BIOPHYSICS AND PHYSICS OF BIOMOLECULES</subject>
    </subj-group>
    <subj-group>
     <subject>МОЛЕКУЛЯРНАЯ БИОФИЗИКА И ФИЗИКА БИОМОЛЕКУЛ</subject>
    </subj-group>
   </article-categories>
   <title-group>
    <article-title xml:lang="en">The role of beta-casein structural state in binding and solubilization of retinol</article-title>
    <trans-title-group xml:lang="ru">
     <trans-title>Роль структурного состояния бета-казеина в его связывающих и солюбилизационных свойствах по отношению к ретинолу</trans-title>
    </trans-title-group>
   </title-group>
   <contrib-group content-type="authors">
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Коннова</surname>
       <given-names>Т А</given-names>
      </name>
      <name xml:lang="en">
       <surname>Konnova</surname>
       <given-names>T A</given-names>
      </name>
     </name-alternatives>
     <email>tatiana.a.konnova@gmail.com</email>
     <xref ref-type="aff" rid="aff-1"/>
    </contrib>
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Файзуллин</surname>
       <given-names>Д А</given-names>
      </name>
      <name xml:lang="en">
       <surname>Faizullin</surname>
       <given-names>D A</given-names>
      </name>
     </name-alternatives>
     <xref ref-type="aff" rid="aff-2"/>
    </contrib>
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Зуев</surname>
       <given-names>Ю Ф</given-names>
      </name>
      <name xml:lang="en">
       <surname>Zuev</surname>
       <given-names>Yu F</given-names>
      </name>
     </name-alternatives>
     <xref ref-type="aff" rid="aff-3"/>
    </contrib>
   </contrib-group>
   <aff-alternatives id="aff-1">
    <aff>
     <institution xml:lang="ru">Казанский институт биохимии и биофизики Казанского научного центра РАН</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Kazan Institute of Biochemistry and Biophysics KazSC RAS</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <aff-alternatives id="aff-2">
    <aff>
     <institution xml:lang="ru">Казанский институт биохимии и биофизики Казанского научного центра РАН</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Kazan Institute of Biochemistry and Biophysics KazSC RAS</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <aff-alternatives id="aff-3">
    <aff>
     <institution xml:lang="ru">Казанский институт биохимии и биофизики Казанского научного центра РАН</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Kazan Institute of Biochemistry and Biophysics KazSC RAS</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <pub-date publication-format="print" date-type="pub" iso-8601-date="2017-06-25T20:22:29+03:00">
    <day>25</day>
    <month>06</month>
    <year>2017</year>
   </pub-date>
   <pub-date publication-format="electronic" date-type="pub" iso-8601-date="2017-06-25T20:22:29+03:00">
    <day>25</day>
    <month>06</month>
    <year>2017</year>
   </pub-date>
   <volume>2</volume>
   <issue>1</issue>
   <fpage>309</fpage>
   <lpage>313</lpage>
   <history>
    <date date-type="received" iso-8601-date="2017-06-20T20:22:29+03:00">
     <day>20</day>
     <month>06</month>
     <year>2017</year>
    </date>
    <date date-type="accepted" iso-8601-date="2017-06-20T20:22:29+03:00">
     <day>20</day>
     <month>06</month>
     <year>2017</year>
    </date>
   </history>
   <self-uri xlink:href="https://rusjbpc.ru/en/nauka/article/54179/view">https://rusjbpc.ru/en/nauka/article/54179/view</self-uri>
   <abstract xml:lang="ru">
    <p>Использование комплекса взаимодополняющих биофизических методов (флуоресцентная, КД- и ИК-спектроскопия, динамическое светорассеяние) позволило изучить корреляцию между агрегатным состоянием (мономеры, ассоциаты), реологическими свойствами белка и вторичной структурой природной и рекомбинантных форм бета-казеина. Получен массив экспериментальных данных о механизмах самоассоциации бета-казеина, уточняющий границы его коллоидного состояния, определены температуры переходов мономер-мицелла, размеры агрегатов природной и модифицированных форм белка. Охарактеризована мицеллообразующая способность и солюбилизационная емкость мицелл бета-казеина по отношению к гидрофобному витамину ретинолу. Проанализировано влияние ионной силы раствора на связывание и термодинамическую стабильность комплексов бета-казеина с гидрофобным лигандом. Рассчитанные константы связывания подтверждают, что связывание в комплексах ретинол-бета-казеин зависит от конформации белковой молекулы и ионной силы раствора. Полученные представления о механизмах конформационных переходов, самоассоциации, взаимодействия бета-казеина с целевыми лигандами на молекулярном уровне, способствуют разработке и созданию эффективных белковых носителей биоактивных добавок, лекарственных препаратов.</p>
   </abstract>
   <trans-abstract xml:lang="en">
    <p>The correlation between the aggregate state (monomers, associates), rheological properties and the secondary structure of the native and recombinant beta-caseins was studied by the complex of biophysical methods (fluorescence, CD and IR spectroscopy, dynamic light scattering). The experimental data on the mechanisms of beta-casein self-association that specifies its colloidal state limits was obtained, the temperature of monomer-micelle transitions, the size of aggregates of protein native and modified forms were determined. Micelle-forming ability and micellar solubilization capacity of beta-casein micelles towards hydrophobic vitamin retinol were characterized. The effect of the low ionic strength of the solution on the binding and thermodynamic stability of beta-casein complexes with a hydrophobic ligand was analyzed. The resulting binding constants confirm that the binding in retinol-beta-casein complexes depends on the conformation of the protein molecule and the ionic strength of the solution. The obtained insights on the mechanisms of conformational transitions, self-association, interaction of beta-casein with target ligands at the molecular level, contribute to the design and development of effective protein carriers of bioactive additives and drugs.</p>
   </trans-abstract>
   <kwd-group xml:lang="ru">
    <kwd>бета-казеин</kwd>
    <kwd>мицеллы</kwd>
    <kwd>самоассоциация</kwd>
    <kwd>критическая концентрация мицеллообразования</kwd>
    <kwd>константа связывания</kwd>
   </kwd-group>
   <kwd-group xml:lang="en">
    <kwd>beta-casein</kwd>
    <kwd>micelle</kwd>
    <kwd>self-association</kwd>
    <kwd>critical micelle concentration (CMC)</kwd>
    <kwd>binding constant</kwd>
   </kwd-group>
  </article-meta>
 </front>
 <body>
  <p></p>
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