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Secretion of circular proteins using sortase. [PDF]
Methods Mol Biol, 2014 Circular proteins occur naturally and have been found in microorganisms, plants, and eukaryotes where they are commonly involved in host defense. Properties of circular proteins include enhanced resistance to exoproteases, increased thermostability, longer life spans, and increased activity. Using an enzymatic approach based on the bacterial sortase A (
Strijbis K, Ploegh HL.
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A straight path to circular proteins. [PDF]
J Biol Chem, 2009 Folding and stability are parameters that control protein behavior. The possibility of conferring additional stability on proteins has implications for their use in vivo and for their structural analysis in the laboratory. Cyclic polypeptides ranging in size from 14 to 78 amino acids occur naturally and often show enhanced resistance toward ...
Antos JM +6 more
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Analysis and classification of circular proteins in CyBase
Peptide Science, 2010 AbstractCyBase is a database dedicated to the study of the sequences and three‐dimensional structures of ribosomally synthesized, backbone cyclized proteins, and their synthetic variants. This article describes CyBase data and tools that are useful in the analysis of circular proteins.
Kaas, Quentin, Craik, David J
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Circular Micro-Proteins and Mechanisms of Cyclization
Current Pharmaceutical Design, 2011 Transpeptidation reactions result in the formation of new peptide bonds and this can occur between two separate peptides or within the one peptide. These reactions are catalyzed by enzymes and when the N- and C-terminus of the one peptide are joined it results in the formation of cyclic proteins. Cyclization via head-to-tail linkage of the termini of a
Conlan, Brendon, Anderson, Marilyn
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Circular dichroism and its uses in biomolecular research - A Review [PDF]
E3S Web of Conferences, 2021 The higher-order structure of proteins as well as their thermal stability can be determined using the circular dichroism (CD). CD is a common approach for swiftly assessing binding, secondary structure, and folding properties of proteins.
Sangeeta, Pathania Anu Radha
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Circular dichroism and magnetic circular dichroism of nitrogenase proteins [PDF]
Proceedings of the National Academy of Sciences, 1979 Circular dichroism (CD) and magnetic circular dichroism (MCD) spectra of nitrogenase components (MoFe protein and Fe protein) from Azotobacter vinelandii (Av) and Klebsiella pneumoniae (Kp) have been obtained in the near infrared—visible—near ultraviolet spectral region.
P J, Stephens +7 more
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SeqCP: A sequence-based algorithm for searching circularly permuted proteins
Computational and Structural Biotechnology Journal, 2023 Circular permutation (CP) is a protein sequence rearrangement in which the amino- and carboxyl-termini of a protein can be created in different positions along the imaginary circularized sequence.
Chi-Chun Chen +4 more
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Biosynthesis of circular proteins in plants [PDF]
The Plant Journal, 2007 SummaryPlant cyclotides are a large family of naturally occurring circular proteins that are produced from linear precursors containing one, two or three cyclotide domains. The mechanism of excision of the cyclotide domains and ligation of the free N‐ and C‐termini to produce the circular peptides has not been elucidated.
Gillon, Amanda Diane. +5 more
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Circular RNAs Could Encode Unique Proteins and Affect Cancer Pathways
Biology, 2023 circRNAs constitute a novel class of RNA, generally considered as non-coding RNAs; nonetheless, their coding potential has been under scrutiny. In this work, we systematically explored the predicted proteins of more than 160,000 circRNAs detected by ...
Francesca Crudele +13 more
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Identification of potential proteins translated from circular RNA splice variants
European Journal of Cell Biology, 2023 Circular RNAs (circRNAs) are covalently closed RNA molecules generated from precursor RNAs by the head-to-tail backsplicing of exons. Hundreds of studies demonstrated that circRNAs are ubiquitously expressed and regulate cellular events by modulating ...
Aniruddha Das +4 more
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