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Force-Clamp Rheometry for Characterizing Protein-based Hydrogels
Published on: August 21, 2018
蛋白质和酸水化的动力学
Kristofer Modig1, Edvards Liepinsh, Gottfried Otting
1Department of Biophysical Chemistry, Lund University, SE-22100 Lund, Sweden.
Journal of the American Chemical Society
|January 8, 2004
概括
像催产素和BPTI这样的生物分子附近的水动力学仅略有减速,大多数水分子的运动速度几乎与散装水一样快. 这项研究揭示了使用磁放松分散的蛋白质水化层的洞察力.
科学领域:
- 生物物理学的生物物理.
- 结构生物学 结构生物学
- 物理化学 物理化学
背景情况:
- 生物过程受到蛋白质表面水的独特特性的影响.
- 了解蛋白质水化动态对于破译生物分子相互作用至关重要.
- 磁放松分散 (MRD) 和核过度调节效应 (NOE) 是研究水动态的关键技术.
研究的目的:
- 为了研究生物分子的水化层中的水分子的动力学.
- 描述循环 (催产素) 和球状蛋白 (BPTI) 对水动态的影响.
- 使用一种新的双极松理论来协调MRD和NOE数据.
主要方法:
- 在2H和17O水核上测量磁放松分散 (MRD).
- 分析了水和蛋白质质子之间的核重置效应 (NOE) 数据.
- 对氧化和BPTI深度超冷溶液的研究.
主要成果:
- 超过95%的生物分子表面的水分子的运动速度仅比散装水慢两倍.
- BPTI的水化层显示出最小的温度依赖性,与小型非极性分子不同.
- 暴露在BPTI上的非极性残留物似乎没有形成类似酸盐的结构.
结论:
- 蛋白质水化层表现出令人惊的快速水动态.
- 围绕BPTI的水的行为表明缺乏类似于克拉特酸盐的疏水性水合.
- 一个新的分子间二极松理论成功地整合了MRD和NOE的发现,澄清了水与蛋白的相互作用.
相关概念视频
What are Proteins?
Overview
Relative Strengths of Conjugate Acid-Base Pairs
Brønsted-Lowry acid-base chemistry is the transfer of protons; thus, logic suggests a relation between the relative strengths of conjugate acid-base pairs. The strength of an acid or base is quantified in its ionization constant, Ka or Kb, which represents the extent of the acid or base ionization reaction. For the conjugate acid-base pair HA / A−, the ionization equilibrium equations and ionization constant expressions are
Polyprotic Acids
Acids are classified by the number of protons per molecule that they can give up in a reaction. Acids such as HCl, HNO3, and HCN that contain one ionizable hydrogen atom in each molecule are called monoprotic acids. Their reactions with water are:
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What are Proteins?
Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight. Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional structure...
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