ProFrost · Theoretical and Numerical Analysis of Antifreeze and Ice Nucleator Proteins:Coarse-Grain Approach for Multiscale Study and Bio-Engineering
„Хоризонт 2020“ — Действия „Мария Склодовска-Кюри“
- Период
- 2018-09-01 → 2020-08-31
- Финансиране от ЕС
- 158 122 €
- Участници
- 1
- Схема
- MSCA-IF-EF-ST
Линиите свързват координатора с партньорите.
Накратко на български
Специални протеини при риби и растения контролират образуването на лед, за да помогнат на организмите да оцелеят при екстремен студ. Разбирането на тези механизми помага при консервирането на органи и храни, както и при подобряване на устойчивостта на култивирани растения.
Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.
Резултати накратко
Theoretical and Numerical Analysis of Antifreeze and Ice Nucleator Proteins:Coarse-Grain Approach for Multiscale Study and Bio-Engineering
In nature life has evolved in order to adapt to a large variety of environmental conditions. In particular, many living beings are capable of surviving in drastic conditions of temperature and pressure, where the water contained in their organism would easily freeze. It is the case, for example, of fishes, insects and plants living in the arctic regions or in desert areas prone to large temperature excursions. Life in such conditions is possible thanks to a special class of "ice-binding" proteins that, together with other molecular mechanisms, can control the ice formation in the cells. The ice binding proteins can prevent the growth of ice crystal (anti-freeze proteins) or enhance it (ice-nucleation proteins). This class of proteins have attracted in recent years the attention of the scientific community given their potential applications in cryo-preservation of tissues and and organs in medicine, storage of frozen foods and lengthening of their shelf life, increasing the freeze tolerance of cultivated plants and farmed fish, production of artificial snow. The exact mechanisms through which these proteins recognize the ice structure from liquid water and how they bind it are still debated. The proposed project ProFrost aimed at filling this gap, shedding light on the physical/chemical features that allow these proteins to bind and control the ice. This knowledge can be exploited to design artificial (bio)molecules with properties similar to the ice-binding proteins.
Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз
Цел на проекта
In nature there are many organisms able to control the ice nucleation rate of water. This ability allows such organisms to adapt to environmental changes, like large temperatures excursions, and to facilitate the search for food.Bio-molecules such as antifreeze proteins (AFPs) and ice nucleator proteins (INPs) are known to influence the ice nucleation rate, a feature that attracts great interest from a wide spectrum of scientific disciplines like biology and atmospheric science, and it offers several technological applications like cryo-preservation of tissues and increasing frozen food shelf life. I propose a new approach, based on a novel combination of water-protein coarse-grain model, able, for a wide range of temperatures and pressures, to deeply explore the configurational space of a water-protein solutions. The ProFrost project aims at defining a novel theoretical framework within which it will be possible to study how the folding properties of AFPs and INPs affect the thermodynamic state point of water. The main goal of the project is to understand the influence of protein interfaces on the dynamical and structural properties of water. The success of this project will pave the way for the computer based design of artificial functionalized protein sequencescapable of influencing the phase of water. This project follows an innovative research line, with a multi-scale approach that combines multiple fields of research, such as physics, biology and chemistry. This research due to its interdisciplinary character and broad interest, has large impact and is often subject of publications on relevant international scientific journals, such as Nature, Science, Proceeding of National Academy of Science, Physical Review Letters. ProFrost will carried out under the supervision Prof Carlos Vega, a leading expert on water, and in collaboration with Prof. Dellago and Dr. Coluzza, expert in modelling and simulations of biophysical systems,
Оригинален текст от CORDIS (на английски).
Участници
- UNIVERSIDAD COMPLUTENSE DE MADRID · MadridКоординаторИспания
Връзки
Данни: CORDIS, © Европейски съюз
