The unfolding of native laminin investigated by atomic force microscopy

Cs Nemes, Jeremy Ramsden and N Rozlosnik

Physica A: Statistical Mechanics and its Applications, 2002, vol. 313, issue 3, 578-586

Abstract: Atomic force microscopy has been used to directly measure the forces required to unfold individual domains of the extracellular matrix protein laminin. The approach–retraction cycles display a characteristic saw-tooth motif. Tooth heights and separations were used to establish a statistical relation between domain unfolding force and domain extension. The extensible domains of laminin require an unfolding force intermediate between previously established values for α-helical and β-sheet domains in other proteins. The relationship between unfolding force and extension for a given domain is not smooth; discrete steps are observed, interpreted as originating from the modularity of the protein structure.

Keywords: Mechanical denaturation; Protein modules; Worm-like chain (search for similar items in EconPapers)
Date: 2002
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Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:313:y:2002:i:3:p:578-586

DOI: 10.1016/S0378-4371(02)00984-6

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