Theoretical study of the conformation of the lipoamide arm in a mutant H protein

Proteins: Structure, Function and Genetics

Volumn 45, Issue 3, 2001, Pages 237-240

  Roche, Olivier ^a,b   Field, Martin J ^a  

^a INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^b F HOFFMANN LA ROCHE LTD   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLYASE; DIHYDROLIPOAMIDE DEHYDROGENASE; GLYCINE DERIVATIVE; METHYLAMINE;

ARTICLE; CONFORMATION; CRYSTALLOGRAPHY; ELECTRICITY; MOLECULAR DYNAMICS; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE IMAGING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN INTERACTION;

ALANINE; AMINO ACID OXIDOREDUCTASES; AMINO ACID SUBSTITUTION; CARRIER PROTEINS; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; GLUTAMIC ACID; GLYCINE DECARBOXYLASE COMPLEX; GLYCINE DECARBOXYLASE COMPLEX H-PROTEIN; GLYCINE DEHYDROGENASE (DECARBOXYLATING); METHYLAMINES; MODELS, MOLECULAR; MUTATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; THERMODYNAMICS; THIOCTIC ACID;

EID: 0035889682     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.1144     Document Type: Article

References (12)

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3. Theoretical study of the conformation of the H-protein lipoamide arm as a function of its terminal group
4. Refined structures at 2 and 2.2 Å resolution of two forms of the H-protein, a lipoamide-containing protein of the glycine decarboxylase complex
5. Investigation of the local structure and dynamics of the H subunit of the mitochondrial glycine decarboxylase using heteronuclear NMR spectroscopy
6. Interaction between the dihydrolipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme complex. II. Crystal structures of H- and L-proteins
7. Structural and functional characterization of H protein mutants of the glycine decarboxylase complex
8. Nonphysical sampling distribution in Monte Carlo free energy estimation: Umbrella sampling
9. The weighted histogram analysis method for free energy on biomolecules. I. The method
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11. All-atom empirical potential for molecular modeling and dynamics studies of proteins
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