Force of an Actin Spring
نویسندگان
چکیده
منابع مشابه
Force of an actin spring.
Cellular movements are produced by forces. Typically, cytoskeletal proteins such as microtubules and actin filaments generate forces via polymerization or in conjunction with molecular motors. However, the fertilization of a Limulus polyphemus egg involves a third type of actin-based cellular engine--a biological spring. During the acrosome reaction, a 60-microm long coiled and twisted bundle o...
متن کاملStructural dynamics of an actin spring.
Actin-based motility in cells is usually associated with either polymerization/depolymerization in the presence of cross-linkers or contractility in the presence of myosin motors. Here, we focus on a third distinct mechanism involving actin in motility, seen in the dynamics of an active actin spring that powers the acrosomal reaction of the horseshoe crab (Limulus polyphemus) sperm. During this...
متن کاملCalcium regulation of an actin spring.
Calcium is essential for many biological processes involved in cellular motility. However, the pathway by which calcium influences motility, in processes such as muscle contraction and neuronal growth, is often indirect and complex. We establish a simple and direct mechanochemical link that shows how calcium quantitatively regulates the dynamics of a primitive motile system, the actin-based acr...
متن کاملLateral force calibration of an atomic force microscope with a diamagnetic levitation spring system
A novel diamagnetic lateral force calibrator D-LFC has been developed to directly calibrate atomic force microscope AFM cantilever-tip or -bead assemblies. This enables an AFM to accurately measure the lateral forces encountered in friction or biomechanical-testing experiments at a small length scale. In the process of development, deformation characteristics of the AFM cantilever assemblies un...
متن کاملPEVK domain of titin: an entropic spring with actin-binding properties.
The PEVK domain of the giant muscle protein titin is a proline-rich sequence with unknown secondary/tertiary structure. Here we compared the force-extension behavior of cloned cardiac PEVK titin measured by single-molecule atomic force spectroscopy with the extensibility of the PEVK domain measured in intact cardiac muscle sarcomeres. The analysis revealed that cardiac PEVK titin acts as an ent...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2007
ISSN: 0006-3495
DOI: 10.1529/biophysj.106.099994