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Effect of a hydrophobic amino acid at position (i −1) on the stability of β-turns in hydrophilic pentapeptides as studied by NMR and molecular mechanics
Effect of a hydrophobic amino acid at position (i −1) on the stability of β-turns in hydrophilic pentapeptides as studied by NMR and molecular mechanics
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Effect of a hydrophobic amino acid at position (i −1) on the stability of β-turns in hydrophilic pentapeptides as studied by NMR and molecular mechanics

Liu, Xiaohong ; Fraga, Serafin ; Otter, Albin ; Kotovych, George ; Scott, Paul G

Canadian journal of chemistry, 1995-07, Vol.73 (7), p.972-980 [Periódico revisado por pares]

Ottawa, Canada: NRC Research Press

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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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