Folding and stretching in a Go-like model of titin

scientific article published on 01 October 2002

Folding and stretching in a Go-like model of titin is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1002/PROT.10087
P698PubMed publication ID12211021

P50authorMarek CieplakQ43023742
P2093author name stringMark O Robbins
Trinh Xuan Hoang
P2860cites workThe Protein Data Bank: a computer-based archival file for macromolecular structuresQ27860989
Contact order, transition state placement and the refolding rates of single domain proteins.Q34464266
P433issue1
P304page(s)114-124
P577publication date2002-10-01
P1433published inProteinsQ7251514
P1476titleFolding and stretching in a Go-like model of titin
P478volume49

Reverse relations

cites work (P2860)
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Q82691584Computational investigation of the effect of thermal perturbation on the mechanical unfolding of titin I27
Q34727575Connecting thermal and mechanical protein (un)folding landscapes
Q33513485Experimental and computational characterization of biological liquid crystals: a review of single-molecule bioassays
Q42960902Inferring the diameter of a biopolymer from its stretching response
Q37462223Insights from coarse-grained Gō models for protein folding and dynamics
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Q21342828Mineral and Protein-Bound Water and Latching Action Control Mechanical Behavior at Protein-Mineral Interfaces in Biological Nanocomposites
Q47424792Multiple molecule effects on the cooperativity of protein folding transitions in simulations
Q35100972Nanomechanics of β-rich proteins related to neuronal disorders studied by AFM, all-atom and coarse-grained MD methods
Q42153432Predicting the order in which contacts are broken during single molecule protein stretching experiments
Q84741725Stretching and twisting of the DNA duplexes in coarse-grained dynamical models
Q73118407Stretching of a polymer below the theta point
Q43111576Toward a molecular understanding of the anisotropic response of proteins to external forces: insights from elastic network models
Q34180201Universality classes in folding times of proteins

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