In silico thermodynamics stability change analysis involved in BH 4 responsive mutations in phenylalanine hydroxylase: QM/MM and MD simulations analysis

Journal of Biomolecular Structure and Dynamics

Volumn 33, Issue 3, 2015, Pages 573-583

  Chadha, Nidhi ^a,b   Tiwari, Anjani K ^a   Kumar, Vikas ^a,b   Milton, Marilyn D ^b   Mishra, Anil K ^a  

^a INSTITUTE OF NUCLEAR MEDICINE AND ALLIED SCIENCES   (India)

^b UNIVERSITY OF DELHI   (India)

Author keywords

Docking; Hydroxylases; MD; Mutation; QM MM; Tetrahydrobiopterin

Indexed keywords

GLUTAMIC ACID; HEME; HISTIDINE; IRON; METALLOPROTEIN; PHENYLALANINE 4 MONOOXYGENASE; TETRAHYDROBIOPTERIN; BIOPTERIN; SAPROPTERIN;

ARTICLE; BINDING AFFINITY; COMPUTER MODEL; COMPUTER PROGRAM; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; GENE MUTATION; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; MUTATIONAL ANALYSIS; PROTEIN FOLDING; QUANTUM MECHANICS; THERMODYNAMICS; ANALOGS AND DERIVATIVES; CHEMISTRY; GENETICS; HUMAN; MISSENSE MUTATION; PROTEIN SECONDARY STRUCTURE; QUANTUM THEORY;

MAMMALIA;

BIOPTERIN; CATALYTIC DOMAIN; HUMANS; MOLECULAR DYNAMICS SIMULATION; MUTATION, MISSENSE; PHENYLALANINE HYDROXYLASE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; QUANTUM THEORY; THERMODYNAMICS;

EID: 84919837701     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2014.897258     Document Type: Article

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