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Journal of the American Chemical Society

Volumn 123, Issue 27, 2001, Pages 6678-6686

Solution structure, dimerization, and dynamics of a lipophilic α/310-helical, Cα-methylated peptide. Implications for folding of membrane proteins

(9) Dehner, A a Planker, E a Gemmecker, G a Broxterman, Q B b Bisson, W b Formaggio, F c Crisma, M c Toniolo, C c Kessler, H a

a TECHNICAL UNIVERSITY OF MUNICH (Germany)

b DSM RESEARCH (Netherlands)

c UNIVERSITY OF PADOVA (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

LIPOPHILIC;

BIOLOGICAL MEMBRANES; COMPUTER SIMULATION; CONFORMATIONS; DIMERIZATION; HYDRODYNAMICS; HYDROGEN BONDS; MOLECULAR DYNAMICS; MONOMERS; PROTEINS; SIMULATED ANNEALING; VAN DER WAALS FORCES;

AMINES;

3 BROMOBENZOYLISOVALYLVALYLISOVALYL ALPHA METHYLVALYL ALPHA METHYLPHENYLALANYL ALPHA METHYLVALYLISOVALYLMETHYLAMINE; HEPTAPEPTIDE; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; DIMERIZATION; DYNAMICS; LIPOPHILICITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN ANALYSIS; PROTEIN FOLDING; SIMULATION; STRUCTURE ANALYSIS;

DIMERIZATION; MEMBRANE LIPIDS; MEMBRANE PROTEINS; METHYLATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; THERMODYNAMICS;

EID: 0034809581 PISSN: 00027863 EISSN: None Source Type: Journal
DOI: 10.1021/ja010635d Document Type: Article

Times cited : (38)

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