Coiled-Coil Nanomechanics and Uncoiling and Unfolding of the Superhelix and α-Helices of Myosin

PDF Version Also Available for Download.

Description

Article on coiled-coil nanomechanics and uncoiling and unfolding of the superhelix and α-helices of myosin.

Physical Description

15 p.

Creation Information

Root, Douglas D.; Yadavalli, Vamsi K.; Forbes, Jeffrey G. & Wang, Kuan January 6, 2006.

Context

This article is part of the collection entitled: UNT Scholarly Works and was provided by the UNT College of Arts and Sciences to the UNT Digital Library, a digital repository hosted by the UNT Libraries. It has been viewed 303 times. More information about this article can be viewed below.

Who

People and organizations associated with either the creation of this article or its content.

Authors

Publisher

Provided By

UNT College of Arts and Sciences

The UNT College of Arts and Sciences educates students in traditional liberal arts, performing arts, sciences, professional, and technical academic programs. In addition to its departments, the college includes academic centers, institutes, programs, and offices providing diverse courses of study.

Contact Us

What

Descriptive information to help identify this article. Follow the links below to find similar items on the Digital Library.

Degree Information

Description

Article on coiled-coil nanomechanics and uncoiling and unfolding of the superhelix and α-helices of myosin.

Physical Description

15 p.

Notes

Abstract: The nanomechanical properties of the coiled-coils of myosin are fundamentally important in understanding muscle assembly and contraction. Force spectra of single molecules of double-headed myosin, single-headed myosin, and coiled-coil tail fragments were acquired with an atomic force microscope and displayed characteristic triphasic force-distance responses to stretch: a rise phase (R) and a plateau phase (P) and an exponential phase (E). The R and P phases arise mainly from the stretching of the coiled-coils, with the hinge region being the main contributor to the rise phase at low force. Only the E phase was analyzable by the worm-like chain model of polymer elasticity. Restrained molecular mechanics simulations on an existing x-ray structure of scallop S2 yielded force spectra with either two or three phases, depending on the mode of stretch. It revealed that coiled-coil chains separate completely near the end of the P phase and the stretching of the unfolded chains gives rise to the E phase. Extensive conformational searching yielded a P phase force near 40 pN that agreed well with the experimental value. We suggest that the flexible and elastic S2 region, particularly the hinge region, may undergo force-induced unfolding and extend reversibly during actomyosin powerstroke.

Subjects

Source

  • Biophysical Journal, 90(8), Biophysical Society, January 6, 2009, pp. 1-15

Language

Item Type

Identifier

Unique identifying numbers for this article in the Digital Library or other systems.

Publication Information

  • Publication Title: Biophysical Journal
  • Volume: 90
  • Issue: 8
  • Page Start: 2852
  • Page End: 2866
  • Peer Reviewed: Yes

Collections

This article is part of the following collection of related materials.

UNT Scholarly Works

Materials from the UNT community's research, creative, and scholarly activities and UNT's Open Access Repository. Access to some items in this collection may be restricted.

What responsibilities do I have when using this article?

When

Dates and time periods associated with this article.

Creation Date

  • January 6, 2006

Added to The UNT Digital Library

  • March 7, 2014, 7:40 a.m.

Description Last Updated

  • Nov. 20, 2023, 1:03 p.m.

Usage Statistics

When was this article last used?

Yesterday: 0
Past 30 days: 0
Total Uses: 303

Interact With This Article

Here are some suggestions for what to do next.

Start Reading

PDF Version Also Available for Download.

International Image Interoperability Framework

IIF Logo

We support the IIIF Presentation API

Root, Douglas D.; Yadavalli, Vamsi K.; Forbes, Jeffrey G. & Wang, Kuan. Coiled-Coil Nanomechanics and Uncoiling and Unfolding of the Superhelix and α-Helices of Myosin, article, January 6, 2006; [Rockville, Maryland]. (https://digital.library.unt.edu/ark:/67531/metadc277177/: accessed February 14, 2025), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; crediting UNT College of Arts and Sciences.

Back to Top of Screen