A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis

Protein Engineering, Design and Selection

Volumn 23, Issue 7, 2010, Pages 499-506

  Hagan, Christine L ^a   Johnson, Russell J K ^a   Dhulesia, Anne ^a   Dumoulin, Mireille ^b   Dumont, Janice ^b   De Genst, Erwin ^a   Christodoulou, John ^a,c   Robinson, Carol V ^a,d   Dobson, Christopher M ^a   Kumita, Janet R ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF LIÈGE   (Belgium)

^c UNIVERSITY COLLEGE LONDON   (United Kingdom)

^d UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

fibril formation; human lysozyme; protein misfolding; systemic amyloidosis

Indexed keywords

AMYLOID DISEASE; CHARACTERISATION; CONFORMATIONAL TRANSITIONS; COOPERATIVITY; FIBRIL FORMATION; GENERIC NATURE; HUMAN LYSOZYME; IN-VITRO; LABELLED PROTEIN; LYSOZYME VARIANTS; MULTIDIMENSIONAL NMR; NATIVE STRUCTURES; NATURALLY OCCURRING; POINT MUTATIONS; PROTEIN MISFOLDING; STRUCTURAL STUDIES; SYSTEMIC AMYLOIDOSIS; WILD-TYPE PROTEINS;

DISEASES; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

ENZYMES;

LYSOZYME;

AMYLOIDOSIS; ARTICLE; FAMILIAL AMYLOIDOSIS; IN VITRO STUDY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH MEASUREMENT; POINT MUTATION; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AMYLOID; AMYLOIDOSIS, FAMILIAL; DEUTERIUM EXCHANGE MEASUREMENT; HUMANS; MODELS, MOLECULAR; MURAMIDASE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; POINT MUTATION; THERMODYNAMICS;

EID: 77955947118     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzq023     Document Type: Article

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