Title:
Steered molecular dynamics studies of titin I1 domain unfolding

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dc.contributor.author Gao, Mu
dc.contributor.author Wilmanns, Matthias
dc.contributor.author Schulten, Klaus
dc.contributor.corporatename Georgia Institute of Technology. Center for the Study of Systems Biology
dc.contributor.corporatename Georgia Institute of Technology. School of Biology
dc.contributor.corporatename Beckman Institute for Advanced Science and Technology
dc.contributor.corporatename University of Illinois at Urbana-Champaign. Dept. of Physics
dc.date.accessioned 2011-11-08T20:58:49Z
dc.date.available 2011-11-08T20:58:49Z
dc.date.issued 2002-12
dc.description © 2002 by the Biophysical Society en_US
dc.description.abstract The cardiac muscle protein titin, responsible for developing passive elasticity and extensibility of muscle, possesses about 40 immunoglobulin-like (Ig) domains in its I-band region. Atomic force microscopy (AFM) and steered molecular dynamics (SMD) have been successfully combined to investigate the reversible unfolding of individual Ig domains. However, previous SMD studies of titin I-band modules have been restricted to I27, the only structurally known Ig domain from the distal region of the titin I-band. In this paper we report SMD simulations unfolding I1, the first structurally available Ig domain from the proximal region of the titin I-band. The simulations are carried out with a view toward upcoming atomic force microscopy experiments. Both constant velocity and constant force stretching have been employed to model mechanical unfolding of oxidized I1, which has a disulfide bond bridging -strands C and E, as well as reduced I1, in which the disulfide bridge is absent. The simulations reveal that I1 is protected against external stress mainly through six interstrand hydrogen bonds between its A and B -strands. The disulfide bond enhances the mechanical stability of oxidized I1 domains by restricting the rupture of backbone hydrogen bonds between the A - and G-strands. The disulfide bond also limits the maximum extension of I1 to 220 Å. Comparison of the unfolding pathways of I1 and I27 are provided and implications to AFM experiments are discussed. en
dc.identifier.citation Gao, M, Wilmanns M, Schulten K. 2002. Steered molecular dynamics studies of titin I1 domain unfolding. Biophysical Journal. 83(6):3435-45. en
dc.identifier.issn 0006-3495
dc.identifier.uri http://hdl.handle.net/1853/41958
dc.language.iso en_US en
dc.publisher Georgia Institute of Technology en
dc.publisher.original Biophysical Society
dc.subject Steered molecular dynamics en
dc.subject Titin en
dc.subject Protein folding en
dc.subject Protein reversible unfolding en
dc.title Steered molecular dynamics studies of titin I1 domain unfolding en_US
dc.type Text
dc.type.genre Article
dspace.entity.type Publication
local.contributor.corporatename College of Sciences
local.contributor.corporatename School of Biological Sciences
local.contributor.corporatename Center for the Study of Systems Biology
relation.isOrgUnitOfPublication 85042be6-2d68-4e07-b384-e1f908fae48a
relation.isOrgUnitOfPublication c8b3bd08-9989-40d3-afe3-e0ad8d5c72b5
relation.isOrgUnitOfPublication d3d635bd-b38e-4ef6-a2d0-0875b9a83e34
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