prikaz prve stranice dokumenta Struktura i funkcija ATP-sintaze
  Download
PDF 301.42 KB
undergraduate thesis
Struktura i funkcija ATP-sintaze
2014. urn:nbn:hr:182:849891
Baranašić, Jurica
Josip Juraj Strossmayer University of Osijek
Department of Chemistry

Cite this document

Baranašić, J. (2014). Struktura i funkcija ATP-sintaze (Undergraduate thesis). Osijek: Josip Juraj Strossmayer University of Osijek, Department of Chemistry. Retrieved from https://urn.nsk.hr/urn:nbn:hr:182:849891

Baranašić, Jurica. "Struktura i funkcija ATP-sintaze." Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Department of Chemistry, 2014. https://urn.nsk.hr/urn:nbn:hr:182:849891

Baranašić, Jurica. "Struktura i funkcija ATP-sintaze." Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Department of Chemistry, 2014. https://urn.nsk.hr/urn:nbn:hr:182:849891

Baranašić, J. (2014). 'Struktura i funkcija ATP-sintaze', Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Department of Chemistry, accessed 17 November 2024, https://urn.nsk.hr/urn:nbn:hr:182:849891

Baranašić J. Struktura i funkcija ATP-sintaze [Undergraduate thesis]. Osijek: Josip Juraj Strossmayer University of Osijek, Department of Chemistry; 2014 [cited 2024 November 17] Available at: https://urn.nsk.hr/urn:nbn:hr:182:849891

J. Baranašić, "Struktura i funkcija ATP-sintaze", Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Department of Chemistry, Osijek, 2014. Available at: https://urn.nsk.hr/urn:nbn:hr:182:849891

Please login to the repository to save this object to your list.
Metadata
TitleStruktura i funkcija ATP-sintaze
AuthorJurica Baranašić
MentorElizabeta Has Schon (mentor)
GranterJosip Juraj Strossmayer University of Osijek
Department of Chemistry
Osijek
Defense date and country2014, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
ATP-sintaza je kompleksni protein odgovoran za katalizu sinteze ATP-a i katalize hidrolize ATP-a. Nalazi se u svim organizmima, od bakterija do čovjeka. Građen je od dva dijela koji rotiraju, F0 i F1. F0 dio je građen od ab2c10-15 podjedinica, ali može imati i još dodatnih podjedinica ovisno o organizmu. F0 dio se nalazi kod pozitivne strane (P), strana sa visokim elektrokemijskim potencijalom protona. U F0 dijelu se događa protok protona uz rotaciju c prstena. F1 dio je građen od α3β3-prstena koji se rotira. F1 dio se također sastoji od γ-, ε- i δ-podjedinice. F1 dio se nalazi kod negativne strane (N), strana sa niskim elektrokemijskim potencijalom protona. Sinteza i hidroliza ATP-a se događa u β podjedinici. U nekom trenutku svaka β podjedinica se nalazi u različitoj konformaciji. Ovakav mehanizam rada ne postoji niti u jednom drugom biološkom sustavu. ATP-sintaza iako je mali protein vrlo je efikasan.
Abstract (english)
ATP synthase is a complex protein. It catalyzes synthesis of ATP and also it catalyzes its hydrolysis. It is found in all organisms, from bacteria to man. It is built from two units that rotate, F0 and F1. F0 consists of ab2c10-15 subunits, but it can also have other additional subunits, depending in which organism it is. F0 is situated on the positive side (P), side with a high electrochemical proton gradient. In F0 happens the rotational flow of protons. F1 is built from α3β3-ring which rotates. It also consists of γ-, ε- and δ-subunits. F1 is situated on the negative side (N), side with a low electrochemical proton gradient. Synthesis and hydrolysis happen in β subunits. In any time of the synthesis or hydrolysis the tree β subunits have different conformations. This mechanism is not found in any other biological system. Although ATP synthase is a small protein it is highly efficient.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:182:849891
Study programmeTitle: Chemistry
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) kemije (sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) kemije)
Type of resourceText
File originBorn digital
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2016-07-13 07:09:54