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In silico and in vitro structure-stability-function relationship of analog peptides of Stigmurin and its antibacterial and antibiofilm activities.
Pharmacol Res
July 2022
Laboratory of Technology and Pharmaceutical Biotechnology (Tecbiofar), Department of Pharmaceutical Sciences, College of Pharmacy, Federal University of Rio Grande do Norte (UFRN), Rua General Gustavo Cordeiro de Farias, S/N, Petrópolis, Natal 59012-570, Brazil. Electronic address:
Multidrug-resistant bacterial infections are a threat to public health worldwide, which boosts the urgent need for pharmacological research for new drugs. Although the peptides without disulfide bridges from scorpions have shown antimicrobial action, usually their toxicity hamper their pharmacological application. Stigmurin is a non-hemolytic cationic peptide from Tityus stigmurus venom with antibacterial effect and toxicity on normal cells.
View Article and Find Full Text PDFThe Bioinorganic Chemistry of Mammalian Metallothioneins.
Chem Rev
December 2021
Departments of Biochemistry and Nutritional Sciences, School of Life Course Sciences, Faculty of Life Sciences and Medicine, King's College London, London SE1 9NH, U.K.
The functions, purposes, and roles of metallothioneins have been the subject of speculations since the discovery of the protein over 60 years ago. This article guides through the history of investigations and resolves multiple contentions by providing new interpretations of the structure-stability-function relationship. It challenges the dogma that the biologically relevant structure of the mammalian proteins is only the one determined by X-ray diffraction and NMR spectroscopy.
View Article and Find Full Text PDFExperimental comparison of energy landscape features of ubiquitin family proteins.
Proteins
March 2020
Department of Chemical Sciences, Tata Institute of Fundamental Research, Mumbai, India.
Small ubiquitin-related modifiers (SUMO1 and SUMO2) are ubiquitin family proteins, structurally similar to ubiquitin, differing in terms of their amino acid sequence and functions. Therefore, they provide a great platform for investigating sequence-structure-stability-function relationship. Here, we used chemical denaturation in comparing the folding-unfolding pathways of the SUMO proteins with their structural homologue ubiquitin (UF45W-pseudo wild-type [WT] tryptophan variant) with structurally analogous tryptophan mutations (SUMO1 [S1F66W], SUMO2 [S2F62W]).
View Article and Find Full Text PDFEmerging role of N- and C-terminal interactions in stabilizing (β/α)8 fold with special emphasis on Family 10 xylanases.
Comput Struct Biotechnol J
June 2014
Plant Transformation Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg, New Delhi - 110067, India.
Xylanases belong to an important class of industrial enzymes. Various xylanases have been purified and characterized from a plethora of organisms including bacteria, marine algae, plants, protozoans, insects, snails and crustaceans. Depending on the source, the enzymatic activity of xylanases varies considerably under various physico-chemical conditions such as temperature, pH, high salt and in the presence of proteases.
View Article and Find Full Text PDFProtein folding simulations: from coarse-grained model to all-atom model.
IUBMB Life
June 2009
National Laboratory of Solid State Microstructure, Nanjing University, Nanjing 210093, China.
Protein folding is an important and challenging problem in molecular biology. During the last two decades, molecular dynamics (MD) simulation has proved to be a paramount tool and was widely used to study protein structures, folding kinetics and thermodynamics, and structure-stability-function relationship. It was also used to help engineering and designing new proteins, and to answer even more general questions such as the minimal number of amino acid or the evolution principle of protein families.
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