Muscle Protein Biophysics and Atomic Force Microscopy

在与NIAMS研究人员的持续合作中(dr。Wang， J.G. Forbes和K. Ma)，原子力显微镜（AFM）以及相关的生物工程和物理科学方法正在被应用于研究肌肉蛋白的生物物理和生理病理。在我们早期工作的基础上，包括AdhE酶和钙调素的AFM结构成像和力响应表征，我们进一步研究了大肌肉蛋白titin （3-4 MDa的大量肽链）和nebulin （600-900 kDa）的行为。正如我们发表的一篇综合综述所述，系统的AFM测量和广泛的数据解释工作正集中在理解titin的PEVK基序在其环境中的弹性上。由此产生的见解现在已经通过平行的圆二色性研究得到了扩展，这些研究使我们提出titin PEVK是一种高度进化的纳米凝胶样熵弹簧，而不是简单的通常假设的熵弹簧。titin在维持骨骼肌和心肌组织和力反应方面的关键功能，以及星云蛋白的自然性质，仍然是高度研究的兴趣。

In this continuing collaboration with NIAMS researchers (Drs. K. Wang, J.G. Forbes and K. Ma), atomic force microscopy (AFM) and related bioengineering and physical science methods are being applied to investigate muscle protein biophysics and physiology/pathologies. On the foundation of our earlier work that included AFM structural imaging and force response characterization of AdhE enzyme and Calmodulin, we have proceeded further on investigating the behaviour of the large muscle proteins titin (a massive peptide chain of 3-4 MDa) and nebulin (600-900 kDa). Systematic AFM measurements with extensive data interpretation effort, as presented in a comprehensive review we have published, are being focused on understanding the elasticity of the PEVK motif of titin in its environment. The resulting insights have now been expanded by parallel circular dichroism studies that lead us to propose titin PEVK as a highly evolved nanoscopic gel-like enthalpic spring, in contrast to a simple commonly assumed entropic spring. The crucial functions of titin in maintaining skeletal and cardiac muscle organization and force responses, as well as the natural of nebulin protein, remain to be of high research interest.