利用量子化学方法,在B3LYP/6-31+G(d)水平上系统考察气相中赖氨酸二肽(lysine dipeptide,LYSD)分子骨架上对二级结构敏感的振动探针——酰胺-I带的振动光谱。通过势能分布(potential energy distribution,PED)分析方法对酰胺-I带振动模...利用量子化学方法,在B3LYP/6-31+G(d)水平上系统考察气相中赖氨酸二肽(lysine dipeptide,LYSD)分子骨架上对二级结构敏感的振动探针——酰胺-I带的振动光谱。通过势能分布(potential energy distribution,PED)分析方法对酰胺-I带振动模式进行指认,探究酰胺-Ⅰ带振动频率与二肽二级结构之间的相关性,为二肽构象态预测提供了有效途径。展开更多
Background:This study was conducted to determine protein molecular structure profiles and quantify the relationship between protein structural features and protein metabolism and bioavailability of blend pel eted prod...Background:This study was conducted to determine protein molecular structure profiles and quantify the relationship between protein structural features and protein metabolism and bioavailability of blend pel eted products(BPP)based on co-products(canola or carinata)from processing with different proportions of pulse pea screenings and lignosulfonate chemical compound.Method:The protein molecular structures were determined using the non-invasive advanced vibrational molecular spectroscopy(ATR-FT/IR)in terms of chemical structure and biofunctional groups of amides(ⅠandⅡ),α-helix andβ-sheet.Results:The results showed that increasing the level of the co-products in BPP significantly increased the spectral intensity of the amide area and amide height.The products exhibited similar protein secondaryα-helix toβ-sheet ratio.The protein molecular structure profiles(amidesⅠandⅡ,α-helix toβ-sheet)were highly associated with protein degradation kinetics and intestinal digestion.In conclusion,the non-invasive vibrational molecular spectroscopy(ATR-FT/IR)could be used to detect inherent structural make-up characteristics in BPP.Conclusion:The molecular structural features related to protein biopolymer were highly associated with protein utilization and metabolism.展开更多
文摘利用量子化学方法,在B3LYP/6-31+G(d)水平上系统考察气相中赖氨酸二肽(lysine dipeptide,LYSD)分子骨架上对二级结构敏感的振动探针——酰胺-I带的振动光谱。通过势能分布(potential energy distribution,PED)分析方法对酰胺-I带振动模式进行指认,探究酰胺-Ⅰ带振动频率与二肽二级结构之间的相关性,为二肽构象态预测提供了有效途径。
基金financially supported by the grants from Sask Pulse Growers,Natural Sciences and Engineering Research Council of Canada(NSERC)the Sask Canola,the Ministry of Agriculture Strategic Research Chair ProgramSask Milk.
文摘Background:This study was conducted to determine protein molecular structure profiles and quantify the relationship between protein structural features and protein metabolism and bioavailability of blend pel eted products(BPP)based on co-products(canola or carinata)from processing with different proportions of pulse pea screenings and lignosulfonate chemical compound.Method:The protein molecular structures were determined using the non-invasive advanced vibrational molecular spectroscopy(ATR-FT/IR)in terms of chemical structure and biofunctional groups of amides(ⅠandⅡ),α-helix andβ-sheet.Results:The results showed that increasing the level of the co-products in BPP significantly increased the spectral intensity of the amide area and amide height.The products exhibited similar protein secondaryα-helix toβ-sheet ratio.The protein molecular structure profiles(amidesⅠandⅡ,α-helix toβ-sheet)were highly associated with protein degradation kinetics and intestinal digestion.In conclusion,the non-invasive vibrational molecular spectroscopy(ATR-FT/IR)could be used to detect inherent structural make-up characteristics in BPP.Conclusion:The molecular structural features related to protein biopolymer were highly associated with protein utilization and metabolism.
