New insights into disordered proteins and regions according to the FOD-M model

Abstract

A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit (chain / domain). The analysis includes all the Homo Sapiens as well as Mus Musculus proteins present in the DisProt database for which the structure is available. In the analysis, the fuzzy oil drop modified model (FOD-M) was used, taking into account the external force field, modified by the presence of other factors apart from polar water, influencing protein structuring. The paper presents an alternative to secondary-structure-based classification of intrinsically disordered regions (IDR). The basis of our classification is the ordering of hydrophobic core as calculated by the FOD-M model resulting in FOD-ordered or FOD-unordered IDRs.

Changes in Rates of Hospitalizations due to Cannabis Harms in Ontario, Canada Before the Legalization of Nonmedical Cannabis: Retrospective Population-level Study Between 2003 and 2017

“…Although our study was not designed to determine the cause of these increases, there are several possible explanations for our findings. First, increases in hospitalizations due to cannabis harms are consistent with data showing a large increase in self-reported cannabis use in the Canadian population 6 . However, data also indicates that self-reported past-year cannabis use in groups of individuals experiencing the largest increase in hospitalizations due to cannabis harms, those aged 15 to 24, have either decreased (aged 15–17) or not changed (18–24) between 2004 and 2017.…”

“…Cannabis-related harms can result from problematic cannabis use leading to dependence (eg, tolerance, time spent using), unhealthy use (eg, abuse, hazardous use, social problems related to use), poisoning (eg, accidental or intentional), and other harms (eg, motor vehicle collision under cannabis influence) 5 . Cannabis use has been increasing over time in Canada with a 60% increase in self-reported past year cannabis use between 2004 (9.4%) and 2017 (14.8%) among those aged 15 and older 6 . Cannabis use varies significantly by age, socioeconomic status, and sex with greater use in young adults and men 6 .…”

“…Cannabis use has been increasing over time in Canada with a 60% increase in self-reported past year cannabis use between 2004 (9.4%) and 2017 (14.8%) among those aged 15 and older 6 . Cannabis use varies significantly by age, socioeconomic status, and sex with greater use in young adults and men 6 . Critically, studies have not considered how cannabis-related harms differ between subgroups over time (eg, young women vs men).…”

New insights on the catalytic center of proteins from peptidylprolyl isomerase group based on the FOD‐M model

“…8 The FOD model and its modified version (FOD-Mtaking into account the external conditions) can be applied to any protein under consideration. This statement is based on the analysis of the large number of proteins, structures of which were also interpreted with respect to their biological activity, namely the downhill, fast-folding, ultra-fast-folding and antifreeze proteins, 21,22 intrinsically disordered proteins, 90 membrane [91][92][93][94] and amyloid proteins, [95][96][97] as well as when studying for example the influence of mutation, 8 complexation 98 or simulation of protein forlding process. 99 FOD model can help to answer many questions depending on the aim of the research.…”

External Force Field for Protein Folding in Chaperonins─Potential Application in In Silico Protein Folding

“…The current analysis focuses on determining the role of the environment that affects protein folding, especially for chaperonin-mediated folding. 38 The starting point is proteins that when folded in an aqueous environment exhibit structuring with a well-defined hydrophobic core with a polar surface (downhill, fast-folding, ultrafast-folding, and antifreeze proteins type II 18 ). These groups of proteins are examples with structures expressed by low parameter values based on the FOD model: RD and K. Proteins described as K = 0.0 were identified.…”