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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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Detalhes bibliográficos
Main Authors: Daley, Margaret E., Sykes, Brian D.
Formato: Artigo
Idioma:Inglês
Publicado em: Wiley-Blackwell 2003
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Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2323928/
https://ncbi.nlm.nih.gov/pubmed/12824479
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