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Intrinsic Disorder as a Natural Preservative: High Levels of Intrinsic Disorder in Proteins Found in the 2600-Year-Old Human Brain

Autor: Aaron S. Mohammed, Vladimir N. Uversky

Publikováno v: Biology, Vol 11, Iss 12, p 1704 (2022)

Proteomic analysis revealed the preservation of many proteins in the Heslington brain (which is at least 2600-year-old brain tissue uncovered within the skull excavated in 2008 from a pit in Heslington, Yorkshire, England). Five of these proteins—�

Externí odkaz: https://doaj.org/article/e277865e04454a528bb07faae0b06a60

Interactions Under Crowding Milieu: Chemical-Induced Denaturation of Myoglobin is Determined by the Extent of Heme Dissociation on Interaction with Crowders

Autor: Khalida Nasreen, Zahoor Ahmad Parray, Shahzaib Ahamad, Faizan Ahmad, Anwar Ahmed, Salman Freeh Alamery, Tajamul Hussain, Md. Imtaiyaz Hassan, Asimul Islam

Publikováno v: Biomolecules, Vol 10, Iss 3, p 490 (2020)

Generally, in vivo function and structural changes are studied by probing proteins in a dilute solution under in vitro conditions, which is believed to be mimicking proteins in intracellular milieu. Earlier, thermal-induced denaturation of myoglobin,

Externí odkaz: https://doaj.org/article/aa30cac417f14b549fef1750c117d9bc

Predicting Protein Conformational Disorder and Disordered Binding Sites

Autor: Ketty C. Tamburrini, Giulia Pesce, Juliet Nilsson, Frank Gondelaud, Andrey V. Kajava, Jean-Guy Berrin, Sonia Longhi

Publikováno v: Data Mining Techniques for the Life Sciences
Data Mining Techniques for the Life Sciences, 2449, Springer US, pp.95-147, 2022, Methods in Molecular Biology, ⟨10.1007/978-1-0716-2095-3_4⟩
Methods in Molecular Biology ISBN: 9781071620946

International audience; In the last two decades it has become increasingly evident that a large number of proteins adopt either a fully or a partially disordered conformation. Intrinsically disordered proteins are ubiquitous proteins that fulfill ess

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4a2f18840e729f470145603af2f8b22
https://hal.science/hal-03834097/document

The intracellular domain of BP180/collagen XVII is intrinsically disordered and partially folds in an anionic membrane lipid-mimicking environment

Autor: M. Kristian Koski, Kaisa Tasanen, Jussi Tuusa, Salla Ruskamo

Publikováno v: Amino Acids. 52:619-627

The trimeric transmembrane collagen BP180, also known as collagen XVII, is an essential component of hemidesmosomes at the dermal–epidermal junction and connects the cytoplasmic keratin network to the extracellular basement membrane. Dysfunction of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fd6bf85ea21df44279465703e10dcea
https://doi.org/10.1007/s00726-020-02840-5