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The Mechanical Properties of Human Angiostatin Can Be Modulated by Means of Its Disulfide Bonds: A Single‐Molecule Force‐Spectroscopy Study
Author(s) -
Bustanji Yasser,
Samorì Bruno
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20020503)41:9<1546::aid-anie1546>3.0.co;2-u
Subject(s) - force spectroscopy , molecule , disulfide bond , chemistry , angiostatin , spectroscopy , pairing , thiol , hydrogen bond , chemical physics , organic chemistry , biochemistry , physics , medicine , quantum mechanics , angiogenesis , superconductivity
The redox environment controls the topology and mechanical properties of angiostatin by modifying the extent of pairing of the three internal disulfide bonds (1–3, see picture) within its five Kringle domains (K1–K5). This situation was revealed by single‐molecule force‐spectroscopy experiments, analysis of the data, which also allowed the distribution of the different thiol/disulfide reduction intermediates to be estimated.