Molecular Mechanism of Adsorption and Structural Behavior ofProteins at Interfaces

蛋白质界面吸附和结构行为的分子机制

基本信息

  • 批准号:
    8913053
  • 负责人:
  • 金额:
    $ 16.55万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
    Continuing Grant
  • 财政年份:
    1990
  • 资助国家:
    美国
  • 起止时间:
    1990-01-01 至 1993-06-30
  • 项目状态:
    已结题

项目摘要

Adsorption of proteins at fluid interfaces play a vital role in many biological, chemical and biotechnological processes. However, the molecular mechanism of adsorption of proteins is not well understood. Specifically, the fundamental questions that need to be investigated are: what are the molecular forces responsible for adsorption and retention of proteins at fluid interfaces and how these forces are affected by the protein conformation and what is the role of bulk water structure in this vital transport process? Thus, the focus of the proposed research is to elucidate: 1. the influence of protein conformation, molecular flexibility and the bulk water structure on adsorption at interfaces; 2. the conformation of proteins in the adsorbed state and its relation to their surface properties; 3. the additivity of polar and apolar groups of peptides on the kinetics and thermodynamics of adsorption at interfaces. The fundamental information obtained from this study will not only enhance understanding of macromolecular adsorption processes, but also will facilitate development of genetic engineering approaches to improve the surface properties of biologically and technologically important proteins.
蛋白质在流体界面上的吸附对蛋白质的形成起着至关重要的作用。 在许多生物、化学和生物技术领域中的作用 流程. 然而,吸附的分子机制 蛋白质的结构还不太清楚。 具体而言是 需要调查的基本问题是: 什么是吸附的分子力 和蛋白质在流体界面的滞留, 这些力受蛋白质构象的影响, 在这个至关重要的过程中, 运输过程? 因此,建议的重点 研究目的是阐明:1. 蛋白质的影响 构象、分子柔性和本体水 界面吸附结构; 2. 的 蛋白质在吸附状态下的构象及其 与其表面性质有关; 3. 可加性 肽的极性和非极性基团的动力学和 界面吸附热力学 从这项研究中获得的基本信息将 不仅加深了对大分子 吸附过程,而且还将促进发展 基因工程的方法来改善表面 生物学和技术上重要的特性 proteins.

项目成果

期刊论文数量(0)
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专利数量(0)

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Srinivasan Damodaran其他文献

Removal of off-flavour-causing precursors in soy protein by concurrent treatment with phospholipase A<sub>2</sub> and cyclodextrins
  • DOI:
    10.1016/j.foodchem.2018.05.045
  • 发表时间:
    2018-10-30
  • 期刊:
  • 影响因子:
  • 作者:
    Dan Zhu;Srinivasan Damodaran
  • 通讯作者:
    Srinivasan Damodaran
Chemical Modification and Structural Analysis of Protein Isolates to Produce Hydrogel using Whitemouth Croaker (Micropogonias furnieri) Wastes
  • DOI:
    10.1007/s12010-011-9250-y
  • 发表时间:
    2011-04-20
  • 期刊:
  • 影响因子:
    3.300
  • 作者:
    Vilásia Guimarães Martins;Jorge Alberto Vieira Costa;Srinivasan Damodaran;Carlos Prentice
  • 通讯作者:
    Carlos Prentice
Enzymological characteristics of pepsinogens and pepsins purified from lizardfish (emSaurida micropectoralis/em) stomach
从蜥鱼(emSaurida micropectoralis/em)胃中纯化的胃蛋白酶原和胃蛋白酶的酶学特性
  • DOI:
    10.1016/j.foodchem.2021.130532
  • 发表时间:
    2022-01-01
  • 期刊:
  • 影响因子:
    9.800
  • 作者:
    Sakonwat Kuepethkaew;Yi Zhang;Hideki Kishimura;Yuya Kumagai;Benjamin K. Simpson;Soottawat Benjakul;Srinivasan Damodaran;Sappasith Klomklao
  • 通讯作者:
    Sappasith Klomklao
Enzymological characteristics of pepsinogens and pepsins purified from lizardfish (<em>Saurida micropectoralis</em>) stomach
  • DOI:
    10.1016/j.foodchem.2021.130532
  • 发表时间:
    2022-01-01
  • 期刊:
  • 影响因子:
  • 作者:
    Sakonwat Kuepethkaew;Yi Zhang;Hideki Kishimura;Yuya Kumagai;Benjamin K. Simpson;Soottawat Benjakul;Srinivasan Damodaran;Sappasith Klomklao
  • 通讯作者:
    Sappasith Klomklao

Srinivasan Damodaran的其他文献

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{{ truncateString('Srinivasan Damodaran', 18)}}的其他基金

Mechanism of Adsorption, Film Formation, and Conformational Stability of Proteins at Liquid Interfaces
蛋白质在液体界面的吸附、成膜和构象稳定性机制
  • 批准号:
    9712197
  • 财政年份:
    1997
  • 资助金额:
    $ 16.55万
  • 项目类别:
    Standard Grant
Adsorption, Film Formation, and Conformational Stability of Proteins at Interfaces
蛋白质在界面处的吸附、成膜和构象稳定性
  • 批准号:
    9315123
  • 财政年份:
    1993
  • 资助金额:
    $ 16.55万
  • 项目类别:
    Continuing Grant
Adsorption of Proteins at Fluid Interfaces: Role of ProteinStructure
蛋白质在流体界面的吸附:蛋白质结构的作用
  • 批准号:
    8616970
  • 财政年份:
    1987
  • 资助金额:
    $ 16.55万
  • 项目类别:
    Continuing Grant

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