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The role of side chain conformational flexibility in surface recognition by Tenebrio molitor antifreeze protein
Two-dimensional nuclear magnetic resonance spectroscopy was used to investigate the flexibility of the threonine side chains in the β-helical Tenebrio molitor antifreeze protein (TmAFP) at low temperatures. From measurement of the (3)J(αβ) (1)H-(1)H scalar coupling constants, the χ(1) angles and pre...
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| Autores principales: | , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
Wiley-Blackwell
2003
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2323928/ https://ncbi.nlm.nih.gov/pubmed/12824479 |
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