检索结果-南通市图书馆

Interactive association between processing induced molecular structure changes and nutrient delivery on a molecular basis,revealed by cutting-edge vibrational biomolecular spectroscopy

引用

Journal of Animal Science and Biotechnology 2020年第1期11卷 211-226页

作者： Aya Ismael Victor Hugo Guevara-Oquendo Basim Refat Peiqiang Yu Ministry of Agriculture Strategic Research Chair(PY)Lab Department of Animal and Poultry ScienceCollege of Agriculture and BioresourcesUniversity of Saskatchewan51 Campus DriveSaskatoonSK S7N 5A8Canada

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 ***: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-***:The results showed that increasing the level of the co-products in BPP significantly increased the spectral intensity of the amide area and amide *** products exhibited similar protein secondaryα-helix toβ-sheet *** protein molecular structure profiles(amidesⅠandⅡ,α-helix toβ-sheet)were highly associated with protein degradation kinetics and intestinal *** conclusion,the non-invasive vibrational molecular spectroscopy(ATR-FT/IR)could be used to detect inherent structural make-up characteristics in ***:The molecular structural features related to protein biopolymer were highly associated with protein utilization and metabolism.

关键词： alpha-helix and beta-sheet Amides(ⅠandⅡ) Biofunctional groups Chemical structure Protein metabolism and bioavailability Protein molecular structure

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

More precise model of <i>α</i>-helix and transmembrane <i>α</i>-helical peptide backbone structure

引用

Journal of Biophysical Chemistry 2012年第4期3卷 295-303页

作者： Walter F. Schmidt Clayton G. Thomas Agricultural Research Service USA Department of Agriculture Beltsville USA Department of Engineering Morgan State University Baltimore USA

The 3-D structure of the β-adrenergic receptor with a molecular weight of 55,000 daltons is available from crystallographic data. Within one of the seven transmembrane ion channel helices in the β2-receptor, one loop of a helix ACADL has previously been proposed as the site that explains β2 activity (fights acute bronchitis) whereas ASADL in the β1-receptor at the corresponding site explains β1-activity (cardiac stimulation). The α-agonist responsible for this selective reaction is only 0.5% of the receptor molecular weight, and only 1.5% of the weight of the trans-membrane portion of the receptor. The understanding of the mechanism by which a small molecule on binding to a site on one single loop of a helix produces a specific agonist activity on an entire transmembrane ion channel is uncertain. A model of an α-helix is presented in which of pitch occurs at angles both smaller and larger than 180° n. Consequently, atomic coordinates in a peptide backbone α-helix match the data points of individual atom (and atom types) in the backbone. More precisely, eleven atoms in peptide backbone routinely equal one loop of a helix, instead of eleven amino acid residues equaling three loops of a helix;therefore, an α-helix can begin (or end) at any specific atom in a peptide backbone, not just at any specific amino acid. Wavefront Topology System and Finite Element Methods calculate this specific helical shape based only upon circumference, pitch, and phase. Only external forces which specifically affect circumference, pitch and/or phase (e.g. from agonist binding) can/will alter the shape of an α-helix.

关键词： helix alpha-helix Circumference Pitch phase peptide backbone Wavefront Topology System Finite Element Method

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

Spontaneous Unfolding and Refolding of Plantaricin α-helix in Molecular Dynamics Simulation

引用

Computational Molecular Bioscience 2019年第1期9卷 27-39页

作者： Shaomin Yan Guang Wu State Key Laboratory of Non-Food Biomass and Enzyme Technology National Engineering Research Center for Non-Food Biorefinery Guangxi Key Laboratory of Bio-Refinery Guangxi Academy of Sciences Nanning China

Antimicrobial peptides are promising therapeutic agents in view of increasing resistance to conventional antibiotics. Antimicrobial peptides usually fold in α-helical, β-sheet, and extended/random-coil structures. The α-helical antimicrobial peptides are often unstructured in aqueous solution but become structured on bacterial membrane. The α-helical structure allows the partitioning into bacterial membrane. Therefore it is important to understand the mechanism of unfolding and refolding of α-helical structure in antimicrobial peptides. It is not very easy to obverse and study the process of unfolding and refolding of α-helical antimicrobial peptides because of their rapidity. Therefore, molecular simulation provides a way to observe and explain this phenomenon. Plantaricin A is a 26 amino-acid antimicrobial pheromone peptide and can spontaneously unfold and refold under physiological condition. This study demonstrated the unfolding and refolding of plantaricin A by means of molecular simulation, and its mechanism was discussed with its implication to the Levinthal paradox.

关键词： alpha-helix Antimicrobial Peptides Protein Folding Plantaricin A

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：