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The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition

Fulton, KF; Buckle, AM; Cabrita, LD; Irving, JA; Butcher, RE; Smith, I; Reeve, S; ... Whisstock, JC; + view all (2005) The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition. JOURNAL OF BIOLOGICAL CHEMISTRY , 280 (9) pp. 8435-8442. 10.1074/jbc.M410206200.

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Type: Article
Title: The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition
DOI: 10.1074/jbc.M410206200
Keywords: Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, HUMAN ALPHA(1)-ANTITRYPSIN, CONFORMATIONAL DISEASES, ACTIVE-SITE, TERNARY COMPLEX, PROTEIN, ANTITHROMBIN, HEPARIN, INHIBITOR, STABILITY, EVOLUTION
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine > Respiratory Medicine
URI: http://discovery.ucl.ac.uk/id/eprint/1426061
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