Роль петлеподібних структур у конформаційній адаптації сироваткового альбуміну людини до зв’язування лігандів

A new conformation of human serum albumin molecule has been found using theoretical conformational analysis methods. One peculiarity of the new conformation as compared to the native structure is a change of Ia domain spatial location with respect to the whole protein globule that is accompanied with a conformational change of the loop-like chain fragment 106–177. The fragment belongs to subdomain Ib and is adjacent to subdomain Ia. The new conformation differs from the original one by the absence of contacts between the fragment 106–177 and subdomain Ia, as well as by lower potential energy and higher solvation. It has been revealed that loop-like structures in proteins may possibly initiate and modulate mobility of domains, and the conformational transition of the chain fragment 106–177 may play essential role in the global conformational change of HSA when binding fatty acids. Further application of the developed model of HSA molecule will allow better understanding the mechanism of the protein structure adaptation to ligand binding.Методами теоретичного конформаційного аналізу знайдено нову конформацію молекули сироваткового альбуміну людини, у якій переорієнтація субдомену Іa у глобулі пов’язана з конформаційним переходом петлеподібної ділянки 106–177. Аргументовано важливу роль такого переходу при утворенні комплексів білка з лігандо

Соотношения раздутия на C2/Z2\mathbb C^2/\mathbb Z_2, получаемые из соотношений раздутия Накаджимы-eшиоки

Исходя из соотношений раздутия Накаджимы-eшиоки с помощью элементарного алгебраического подхода доказаны билинейные соотношения на статсуммы Некрасова, возникающие при изучении тау-функций квантовых $q$-деформированных уравнений Пенлеве. Дополнительно с помощью этого подхода доказаны некоторые симметрийные соотношения на статсуммы Некрасова, модифицированные членом Черна-Саймонса.</jats:p

The Role of Loop-like Structures in the Conformational Adaptation of Human Serum Albumin to Ligands Binding.

Методами теоретичного конформаційного аналізу знайдено нову конформацію молекули сироваткового альбуміну людини, у якій переорієнтація субдомену Іa у глобулі пов’язана з конформаційним переходом петле- подібної ділянки 106–177. Аргументовано важливу роль такого переходу при утворенні комплексів білка з лігандом. A new conformation of human serum albumin molecule has been found using theoretical conformational analysis methods. One peculiarity of the new conformation as compared to the native structure is a change of Ia domain spatial location with respect to the whole protein globule that is accompanied with a conformational change of the loop-like chain fragment 106–177. The fragment belongs to subdomain Ib and is adjacent to subdomain Ia. The new conformation differs from the original one by the absence of contacts between the fragment 106–177 and subdomain Ia, as well as by lower potential energy and higher solvation. It has been revealed that loop-like structures in proteins may possibly initiate and modulate mobility of domains, and the conformational transition of the chain fragment 106–177 may play essential role in the global conformational change of HSA when binding fatty acids. Further application of the developed model of HSA molecule will allow better understanding the mechanism of the protein structure adaptation to ligand bindin

Optical Biomedical Imaging Reveals Criteria for Violated Liver Regenerative Potential

To reduce the risk of post-hepatectomy liver failure in patients with hepatic pathologies, it is necessary to develop an approach to express the intraoperative assessment of the liver’s regenerative potential. Traditional clinical methods do not enable the prediction of the function of the liver remnant. Modern label-free bioimaging, using multiphoton microscopy in combination with second harmonic generation (SHG) and fluorescence lifetime imaging microscopy (FLIM), can both expand the possibilities for diagnosing liver pathologies and for assessing the regenerative potential of the liver. Using multiphoton and SHG microscopy, we assessed the structural state of liver tissue at different stages of induced steatosis and fibrosis before and after 70% partial hepatectomy in rats. Using FLIM, we also performed a detailed analysis of the metabolic state of the hepatocytes. We were able to determine criteria that can reveal a lack of regenerative potential in violated liver, such as the presence of zones with reduced NAD(P)H autofluorescence signals. Furthermore, for a liver with pathology, there was an absence of the jump in the fluorescence lifetime contributions of the bound form of NADH and NADPH the 3rd day after hepatectomy that is characteristic of normal liver regeneration. Such results are associated with decreased intensity of oxidative phosphorylation and of biosynthetic processes in pathological liver, which is the reason for the impaired liver recovery. This modern approach offers an effective tool that can be successfully translated into the clinic for express, intraoperative assessment of the regenerative potential of the pathological liver of a patient.</jats:p