KNOWLEDGE AND PRACTICE REGARDING FOOT CARE AMONG TYPE 2 DIABETES MELLITUS PATIENTS AT A TERTIARY CARE HOSPITAL IN COASTAL SOUTH INDIA

Objective: The present study was designed to assess the knowledge and practice among diabetic patients in a tertiary care hospital regarding diabeticfoot care.Methods: A cross-sectional study was conducted in government district hospital of Mangalore in the month of January 2014. A pre-designed semistructuredquestionnairewasused tocollectthe informationpertainingtotheknowledgeand practicesofthediabetic patients regardingfootcare.Thecollecteddata wereanalyzedusing Statistical PackagesforSocial Sciences version11.5.The resultsobtained wereexpressedin proportions.Results: A total of 133 subjects were assessed regarding their knowledge and practice regarding diabetic foot care. Around three-fourth (75.2%) ofparticipants had adequate knowledge. More than half (55.5%) of the subjects had adequate practice. No significant association was found betweenstudy variables such as gender, socioeconomic status, and education status with awareness regarding diabetic foot care in the present study (p>0.05).Gender, socioeconomic, and educational statuses were found to be significantly associated with diabetic foot care practices.Conclusion: The gap between knowledge and practice regarding self-care among diabetic patients can be bridged by providing continuous healtheducation by the health workers. Foot care should be promoted at all available opportunities whenever the patient comes in contact with the health system.Keywords: Mangalore, Foot care, Diabetes

Metamorphic proteins: the Janus proteins of structural biology

The structural paradigm that the sequence of a protein encodes for a unique three-dimensional native fold does not acknowledge the intrinsic plasticity encapsulated in conformational free energy landscapes. Metamorphic proteins are a recently discovered class of biomolecules that illustrate this plasticity by folding into at least two distinct native state structures of comparable stability in the absence of ligands or cofactors to facilitate fold-switching. The expanding list of metamorphic proteins clearly shows that these proteins are not mere aberrations in protein evolution, but may have actually been a consequence of distinctive patterns in selection pressure such as those found in virus–host co-evolution. In this review, we describe the structure–function relationships observed in well-studied metamorphic protein systems, with specific focus on how functional residues are sequestered or exposed in the two folds of the protein. We also discuss the implications of metamorphosis for protein evolution and the efforts that are underway to predict metamorphic systems from sequence properties alone

Engineering Order and Cooperativity in a Disordered Protein

Structural disorder in proteins arises from a complex interplay between weak hydrophobicity and unfavorable electrostatic interactions. The extent to which the hydrophobic effect contributes to the unique and compact native state of proteins is, however, confounded by large compensation between multiple entropic and energetic terms. Here we show that protein structural order and cooperativity arise as emergent properties upon hydrophobic substitutions in a disordered system with non-intuitive effects on folding and function. Aided by sequence–structure analysis, equilibrium, and kinetic spectroscopic studies, we engineer two hydrophobic mutations in the disordered DNA-binding domain of CytR that act synergistically, but not in isolation, to promote structure, compactness, and stability. The double mutant, with properties of a fully ordered domain, exhibits weak cooperativity with a complex and rugged conformational landscape. The mutant, however, binds cognate DNA with an affinity only marginally higher than that of the wild type, though nontrivial differences are observed in the binding to noncognate DNA. Our work provides direct experimental evidence of the dominant role of non-additive hydrophobic effects in shaping the molecular evolution of order in disordered proteins and vice versa, which could be generalized to even folded proteins with implications for protein design and functional manipulation.This work was supported by Wellcome Trust/DBT India Alliance Intermediate Fellowship IA/I/15/1/501837 to A.N.N. A.S. acknowledges the Department of Science and Technology, India, for the Ramanujan Fellowship

To what extent is alcohol consumption in social gatherings associated with observance of COVID-19 restrictions?:A rapid review

BACKGROUND: Pre-pandemic research found a connection between alcohol consumption and reduced physical distancing among strangers. Understanding the association between alcohol consumption at social gatherings and observance of COVID-19 restrictions can help inform policy related to the safe operation of public spaces where alcohol is typically consumed, as well as guidance related to the safe conduct of social events in private spaces. METHODS: We conducted a rapid review using adapted systematic review methods to explore the association between alcohol consumption in social gatherings and compliance with COVID-19 public health measures and produced a narrative synthesis of our findings. We ran searches in eleven health-related databases (MEDLINE, PubMed, CINAHL, Scopus, Embase (Ovid), ProQuest Public Health, ProQuest Coronavirus, Global Health (Ovid), WHO COVID-19 literature database, PsycInfo (Ovid) and ASSIA) between July 9, 2021, and July 31, 2021. We assessed methodological quality using the relevant Joanna Briggs Institute (JBI) checklists. This review was conducted and reported in accordance with PRISMA-P guidelines. RESULTS: We identified 7936 studies from the searches. After title, abstract and full-text review, three cross-sectional studies were eligible for inclusion. One study found that people who adhered strongly to physical distancing rules were engaged in about 40% fewer weekly drinks and 60% fewer heavy episodic drinking occasions in a week than people who adhered poorly to physical distancing rules (P < 0.01). One study found that people who reported low-risk alcohol consumption patterns had a higher chance of adhering to hand hygiene measures than those who reported high-risk alcohol consumption (odds ratio (OR) = 4.24, 95% confidence interval (CI) = 1.08-16.64). No other statistically significant results on patterns of alcohol consumption and compliance with individual public health measures or with non-pharmaceutical interventions (NPIs) were found. The direction of effect between alcohol consumption and non-adherence to NPIs and the effect of confounding factors has not been established. The quality of studies found was low to moderate, with risk of recall bias and selection bias due to study design; and the extent to which those studies can be generalised beyond their original settings may be limited. CONCLUSIONS: Despite existing evidence suggesting an association between alcohol consumption, reduced physical distancing, and increased social interaction, we found few studies of variable quality exploring the relationship between alcohol consumption and compliance with public health measures. A possible association between higher-risk alcohol behaviours and lower compliance with certain NPIs was suggested, but the direction of effect is unknown, and further studies are required to confirm this finding

Engineering Order and Cooperativity in a Disordered Protein

Structural disorder in proteins arises from a complex interplay between weak hydrophobicity and unfavorable electrostatic interactions. The extent to which the hydrophobic effect contributes to the unique and compact native state of proteins is, however, confounded by large compensation between multiple entropic and energetic terms. Here we show that protein structural order and cooperativity arise as emergent properties upon hydrophobic substitutions in a disordered system with non-intuitive effects on folding and function. Aided by sequence-structure analysis, equilibrium, and kinetic spectroscopic studies, we engineer two hydrophobic mutations in the disordered DNA-binding domain of CytR that act synergistically, but not in isolation, to promote structure, compactness, and stability. The double mutant, with properties of a fully ordered domain, exhibits weak cooperativity with a complex and rugged conformational landscape. The mutant, however, binds cognate DNA with an affinity only marginally higher than that of the wild type, though nontrivial differences are observed in the binding to noncognate DNA. Our work provides direct experimental evidence of the dominant role of non-additive hydrophobic effects in shaping the molecular evolution of order in disordered proteins and vice versa, which could be generalized to even folded proteins with implications for protein design and functional manipulation