Protein Adsorption Tuned by Multivalent Ions (PATMI):Connecting Bulk to Interface Behaviour by Controlling Interactions
多价离子调节的蛋白质吸附 (PATMI):通过控制相互作用将体相与界面行为联系起来
基本信息
- 批准号:431858909
- 负责人:
- 金额:--
- 依托单位:
- 依托单位国家:德国
- 项目类别:Research Grants
- 财政年份:
- 资助国家:德国
- 起止时间:
- 项目状态:未结题
- 来源:
- 关键词:
项目摘要
This proposal aims to employ the rich bulk phase behaviour of protein solutions including re-entrant condensation mediated by multivalent ions to elucidate the fundamentals of protein adsorption at interfaces beyond simple charge screening.This qualitatively new behaviour will be explored both at equilibrium (i.e. adsorption isotherms will be determined along with the equilibrium structures) and dynamically (and therefore prior to equilibrium, i.e. the adsorption kinetics will be investigated), with particular attention to clarify the role of surface-induced nucleation and its importance for protein crystallisation.We aim to connect the interface behaviour to the interactions controlled by multivalent ions and the bulk behaviour within the concept of ion-activated patches.We make use of our expertise in surface analysis techniques, such as ellipsometry, QCM-D, FTIRRAS/ATR and in particular neutron and X-ray scattering, which allow a detailed determination of the adsorbed layer structure at the molecular level.
该提案旨在采用蛋白质溶液的丰富体积相位行为,包括由多价离子介导的重进入凝结,以阐明在超出简单充电筛选的范围内蛋白质吸附的基本原理。在质量上,既定的新行为均应在平衡处探索与均衡的均衡(即,在均衡的结构中都可以在均衡中确定均等(即,均一度均具有均匀的启发性),从而在均等均设有动动脉群,因此,一式动脉均取得了启动(即),因此,均一度的均匀效果(即),因此,在均衡(即),均应依次(即)均匀(即),均应在均衡状态。 adsorption kinetics will be investigated), with particular attention to clarify the role of surface-induced nucleation and its importance for protein crystallisation.We aim to connect the interface behaviour to the interactions controlled by multivalent ions and the bulk behaviour within the concept of ion-activated patches.We make use of our expertise in surface analysis techniques, such as ellipsometry, QCM-D, FTIRRAS/ATR and in particular中子和X射线散射,可以详细测定分子水平的吸附层结构。
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Professor Dr. Frank Schreiber其他文献
Professor Dr. Frank Schreiber的其他文献
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{{ truncateString('Professor Dr. Frank Schreiber', 18)}}的其他基金
Exploring the limits of real-time studies of growth of molecular and hybrid systems
探索分子和混合系统生长实时研究的局限性
- 批准号:
419187842 - 财政年份:2019
- 资助金额:
-- - 项目类别:
Research Grants
Static and dynamic properties of antibody proteins in solution - the effects of crowding and charge-tuning
溶液中抗体蛋白的静态和动态特性 - 拥挤和电荷调节的影响
- 批准号:
316738961 - 财政年份:2016
- 资助金额:
-- - 项目类别:
Research Grants
Diffusion in protein solutions: the effect of crowding, temperature and charges
蛋白质溶液中的扩散:拥挤、温度和电荷的影响
- 批准号:
240526267 - 财政年份:2013
- 资助金额:
-- - 项目类别:
Research Grants
In situ and real-time investigations of organic semiconductor film growth
有机半导体薄膜生长的原位实时研究
- 批准号:
99734980 - 财政年份:2009
- 资助金额:
-- - 项目类别:
Research Grants
Two-Components Colloidal Solutions: Tuning the Interactions of Functionalized Nanoparticles with Proteins
双组分胶体溶液:调节功能化纳米粒子与蛋白质的相互作用
- 批准号:
123578767 - 财政年份:2009
- 资助金额:
-- - 项目类别:
Research Grants
Röntgenstreuungsuntersuchungen an organisch-anorganischen Grenzflächen
有机-无机界面的X射线散射研究
- 批准号:
5304886 - 财政年份:2001
- 资助金额:
-- - 项目类别:
Priority Programmes
Dynamics, kinetics and assembly of model intrinsically disordered proteins from a polymer physics perspective
从聚合物物理学的角度研究模型本质无序蛋白质的动力学、动力学和组装
- 批准号:
490662871 - 财政年份:
- 资助金额:
-- - 项目类别:
Research Grants
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