Детальный поиск
Отменить
Найденный: 5 Экземпляр 0.001 sn
- Вы можете использовать опцию И / ИЛИ / НЕ для критериев, которые вы хотите добавить или.
- Вы можете вернуться к обычному поиску, нажав кнопку Отмена.
Фильтры
Фильтры
Найденный: 5 Экземпляр 0.001 sn
Источник : Journal of Biomolecu ... ✕Базы данных : Scopus ✕
Коллекция [1]
Ученые [1]
Устойчивое развитие ООН [5]
Факультет / Институт [1]
Вид публикации [2]
Год публикации [3]
Язык [1]
Источник [1]
Базы данных [3]
Вид индекса [2]
Издатель [1]
Кафедра [1]
Национальный/Международный [1]
Тематический рубрикатор [26]
Доступ к файлам

Comparative modeling and enzymatic affinity of novel haloacid dehalogenase from Bacillus megaterium strain BHS1 isolated from alkaline Blue Lake in Turkey

Yılmaz KAYA

This study presents the initial structural model of L-haloacid dehalogenase (DehLBHS1) from Bacillus megaterium BHS1, an alkalotolerant bacterium known for its ability to degrade halogenated environmental pollutants. The model provides insights into the structural features of DehLBHS1 and expands our understanding of the enzymatic mechanisms involved in the degradation of these hazardous pollutants. Key amino acid residues (Arg40, Phe59, Asn118, Asn176, and Trp178) in DehLBHS1 were identified to play critical roles in catalysis and molecular recognition of haloalkanoic acid, essential for effi ...Более

Статья 2023 Fen Fakültesi Journal of Biomolecular Structure and Dynamics42 ( 3 ) 54 Просмотры
Доступ к файлам

Biodegradation of 3-chloropropionic acid (3-CP) by Bacillus cereus WH2 and its in silico enzyme-substrate docking analysis

Yılmaz KAYA

KeyWords Plus:ALPHA-HALOALKANOIC ACID; DEHALOGENASE; DEGRADATION

Письмо 2019 Fen Fakültesi Journal of Biomolecular Structure and Dynamics38 ( 11 ) 136 Просмотры
Доступ к файлам

Haloadaptation: insights from comparative modeling studies between halotolerant and non-halotolerant dehalogenases

Yılmaz KAYA

Halophiles are extremophilic microorganisms that grow optimally at high salt concentrations by producing a myriad of equally halotolerant enzymes. Structural haloadaptation of these enzymes adept to thriving under high-salt environments, though are not fully understood. Herein, the study attempts an in silico investigation to identify and comprehend the evolutionary structural adaptation of a halotolerant dehalogenase, DehHX (GenBank accession number: KR297065) of the halotolerant Pseudomonas halophila, over its non-halotolerant counterpart, DehMX1 (GenBank accession number KY129692) produced ...Более

Статья 2019 Fen Fakültesi Journal of Biomolecular Structure and Dynamics38 ( 12 ) 113 Просмотры
Доступ к файлам

Substrate docking and molecular dynamic simulation for prediction of fungal enzymes from Trichoderma species-assisted extraction of nanocellulose from oil palm leaves

Yılmaz KAYA

Fungi of the Trichoderma species are valued industrial enzymes in support of the

Статья 2019 Fen Fakültesi Journal of Biomolecular Structure and Dynamics38 ( 14 ) 132 Просмотры
Доступ к файлам

Molecular docking and molecular dynamics simulations studies on beta-glucosidase and xylanase Trichoderma asperellum to predict degradation order of cellulosic components in oil palm leaves for nanocellulose preparation

Yılmaz KAYA

Literature has shown that oil palm leaves (OPL) can be transformed into nanocellulose (NC) by fungal lignocellulosic enzymes, particularly those produced by the Trichoderma species. However, mechanism of beta-glucosidase and xylanase selectivity to degrade lignin, hemicellulose and cellulose in OPL for NC production remains relatively vague. The study aimed to comprehend this aspect by an in silico approach of molecular docking, molecular dynamics (MD) simulation and Molecular-mechanics Poisson-Boltzmann surface area (MM-PBSA) analysis, to compare interactions between the beta-glucosidase- and ...Более

Статья 2020 Fen Fakültesi Journal of Biomolecular Structure and Dynamics39 ( 7 ) 77 Просмотры
Наши обязательства и политика в отношении файлов cookie подпадает под действие закона ТР защите персональных данных № 6698.
Да
creativecommons
Bu site altında yer alan tüm kaynaklar Creative Commons Alıntı-GayriTicari-Türetilemez 4.0 Uluslararası Lisansı ile lisanslanmıştır.
Platforms