Topological diversity of artificial β-barrels in water

Chirality

Volumn 13, Issue 3, 2001, Pages 170-176

  Das, Gopal ^a   Matile, Stefan ^a  

^a UNIVERSITY OF GENEVA   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AMPHOPHILE; DETERGENT; GLUTAMYLLEUCYLGLUTAMIC ACID; GUANIDINE; LYSYLLEUCYLLYSINE; TRIPEPTIDE; UNCLASSIFIED DRUG; WATER;

ARTICLE; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE;

PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEINS; THERMODYNAMICS; WATER;

EID: 0035114710     PISSN: 08990042     EISSN: None     Source Type: Journal    
DOI: 10.1002/1520-636X(2001)13:3<170::AID-CHIR1016>3.0.CO;2-6     Document Type: Article

References (6)

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2. Compare also: Fülöp V, Jones DT. β-Propellers: structural rigidity and functional diversity. Curr Opin Struct Biol 1999;9:715-721.
3. Van der Goot FG. Plasticity of the transmembrane β-barrel. Trends Microbiol 2000;8:89-90.
4. Buchanan SK. β-Barrel proteins from bacterial outer membranes: structure, function and refolding. Curr Opin Struct Biol 1999;9:445-461.
5. Babbitt PC, Gerlt JA. Understanding enzyme superfamilies. J Biol Chem 1997;272:30591-30594.
6. Hecht MH. De novo design of β-sheet proteins. Proc Natl Acad Sci USA 1994;91:8729-8730.