Mechanical Strength of 17 134 Model Proteins and Cysteine Slipknots
نویسندگان
چکیده
منابع مشابه
Mechanical Strength of 17 134 Model Proteins and Cysteine Slipknots
A new theoretical survey of proteins' resistance to constant speed stretching is performed for a set of 17,134 proteins as described by a structure-based model. The proteins selected have no gaps in their structure determination and consist of no more than 250 amino acids. Our previous studies have dealt with 7510 proteins of no more than 150 amino acids. The proteins are ranked according to th...
متن کاملRefolding Process of Cysteine-Rich Proteins: Chitinase as a Model
Background: Recombinant proteins overexpressed in E. coli are usually deposited in inclusion bodies. Cysteines in the protein contribute to this process. Inter- and intra- molecular disulfide bonds in chitinase, a cysteine-rich protein, cause aggregation when the recombinant protein is overexpressed in E. coli. Hence, aggregated proteins should be solubilized and allowed to refold to obtain nat...
متن کاملFormation of Cystine Slipknots in Dimeric Proteins
We consider mechanical stability of dimeric and monomeric proteins with the cystine knot motif. A structure based dynamical model is used to demonstrate that all dimeric and some monomeric proteins of this kind should have considerable resistance to stretching that is significantly larger than that of titin. The mechanisms of the large mechanostability are elucidated. In most cases, it originat...
متن کاملdetermination of some physical and mechanical properties red bean
چکیده: در این تحقیق، برخی خواص فیزیکی و مکانیکی لوبیا قرمز به-صورت تابعی از محتوی رطوبت بررسی شد. نتایج نشان داد که رطوبت بر خواص فیزیکی لوبیا قرمز شامل طول، عرض، ضخامت، قطر متوسط هندسی، قطر متوسط حسابی، سطح تصویر شده، حجم، چگالی توده، تخلخل، وزن هزار دانه و زاویه ی استقرار استاتیکی در سطح احتمال 1 درصد اثر معنی داری دارد. به طوری که با افزایش رطوبت از 54/7 به 12 درصد بر پایه خشک طول، عرض، ضخام...
15 صفحه اولrefolding process of cysteine-rich proteins: chitinase as a model
background: recombinant proteins overexpressed in e. coli are usually deposited in inclusion bodies. cysteines in the protein contribute to this process. inter- and intra- molecular disulfide bonds in chitinase, a cysteine-rich protein, cause aggregation when the recombinant protein is overexpressed in e. coli. hence, aggregated proteins should be solubilized and allowed to refold to obtain nat...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: PLoS Computational Biology
سال: 2009
ISSN: 1553-7358
DOI: 10.1371/journal.pcbi.1000547