Solution studies of chymotrypsin inhibitor-2 glutamine insertion mutants show no interglutamine interactions

Biochemical and Biophysical Research Communications

Volumn 280, Issue 3, 2001, Pages 855-860

  Gordon Smith, Duncan J ^a   Carbajo, Rodrigo J ^a   Stott, Kelvin ^a   Neuhaus, David ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN INHIBITOR; NITROGEN 15; POLYGLUTAMINE;

ARTICLE; DEGENERATIVE DISEASE; ESCHERICHIA COLI; GENE MUTATION; HUNTINGTON CHOREA; KENNEDY DISEASE; MOLECULAR DYNAMICS; NEUROLOGIC DISEASE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE; TRINUCLEOTIDE REPEAT;

EID: 0034814752     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.4196     Document Type: Article

References (12)

1. Polar zippers
2. Glutamine repeats as polar zippers - Their possible role in inherited neurodegenerative diseases
3. Polar zippers - Their role in human disease
4. Glutamine repeats and inherited neurodegenerative diseases: Molecular aspects
5. Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates
6. Crystal structure of a dimeric chymotrypsin inhibitor-2 mutant containing an inserted glutamine repeat
7. Incorporation of glutamine repeats makes protein oligomerize - Implications for neurodegenerative diseases
8. 15N NMR relaxation measurements
9. 15N chemical shift referencing in biomolecular NMR
10. Sequence specific assignment of the proton nuclear magnetic resonance spectrum of barley serine proteinase inhibitor-2
11. Generation of a family of protein fragments for structure-folding studies. 1. Folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue
12. Random coil conformation for extended polyglutamine stretches in aqueous soluble monomeric peptides