Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease

Biophysical Journal

Volumn 101, Issue 9, 2011, Pages 2260-2266

  Hazy, E ^a   Bokor, M ^b   Kalmar, L ^a   Gelencser, A ^a   Kamasa, P ^b   Han, K H ^c   Tompa, K ^b   Tompa, P ^a  

^a INSTITUTE OF ENZYMOLOGY   (Hungary)

^b INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^c Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; MUTANT PROTEIN; WATER;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARKINSON DISEASE; POINT MUTATION; PROTEIN TERTIARY STRUCTURE; TEMPERATURE;

ALPHA-SYNUCLEIN; AMINO ACID SUBSTITUTION; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR DYNAMICS SIMULATION; MUTANT PROTEINS; PARKINSON DISEASE; POINT MUTATION; PROTEIN STRUCTURE, TERTIARY; TEMPERATURE; WATER;

EID: 80455155187     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.08.052     Document Type: Article

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