{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T01:23:51Z","timestamp":1783473831049,"version":"3.55.0"},"reference-count":105,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2023,7,6]],"date-time":"2023-07-06T00:00:00Z","timestamp":1688601600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"government assignment for Federal Research Center Kazan Scientific Center of the Russian Academy of Sciences","award":["PRIORITY-2030"],"award-info":[{"award-number":["PRIORITY-2030"]}]},{"name":"Kazan Federal University Strategic Academic Leadership Program","award":["PRIORITY-2030"],"award-info":[{"award-number":["PRIORITY-2030"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Intracellular environment includes proteins, sugars, and nucleic acids interacting in restricted media. In the cytoplasm, the excluded volume effect takes up to 40% of the volume available for occupation by macromolecules. In this work, we tested several approaches modeling crowded solutions for protein diffusion. We experimentally showed how the protein diffusion deviates from conventional Brownian motion in artificial conditions modeling the alteration of medium viscosity and rigid spatial obstacles. The studied tracer proteins were globular bovine serum albumin and intrinsically disordered \u03b1-casein. Using the pulsed field gradient NMR, we investigated the translational diffusion of protein probes of different structures in homogeneous (glycerol) and heterogeneous (PEG 300\/PEG 6000\/PEG 40,000) solutions as a function of crowder concentration. Our results showed fundamentally different effects of homogeneous and heterogeneous crowded environments on protein self-diffusion. In addition, the applied \u201ctracer on lattice\u201d model showed that smaller crowding obstacles (PEG 300 and PEG 6000) create a dense net of restrictions noticeably hindering diffusing protein probes, whereas the large-sized PEG 40,000 creates a \u201cless restricted\u201d environment for the diffusive motion of protein molecules.<\/jats:p>","DOI":"10.3390\/ijms241311148","type":"journal-article","created":{"date-parts":[[2023,7,7]],"date-time":"2023-07-07T01:41:36Z","timestamp":1688694096000},"page":"11148","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Effects of Homogeneous and Heterogeneous Crowding on Translational Diffusion of Rigid Bovine Serum Albumin and Disordered Alfa-Casein"],"prefix":"10.3390","volume":"24","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9006-4160","authenticated-orcid":false,"given":"Aleksandra M.","family":"Kusova","sequence":"first","affiliation":[{"name":"Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center, Russian Academy of Sciences, Lobachevsky Str. 2\/31, Kazan 420111, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5836-9562","authenticated-orcid":false,"given":"Ilnaz T.","family":"Rakipov","sequence":"additional","affiliation":[{"name":"Institute of Chemistry, Kazan Federal University, Kremlevskaya Str. 18, Kazan 420008, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6715-2530","authenticated-orcid":false,"given":"Yuriy F.","family":"Zuev","sequence":"additional","affiliation":[{"name":"Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center, Russian Academy of Sciences, Lobachevsky Str. 2\/31, Kazan 420111, Russia"},{"name":"Institute of Chemistry, Kazan Federal University, Kremlevskaya Str. 18, Kazan 420008, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,7,6]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3429","DOI":"10.1021\/jz401817x","article-title":"Effects of Macromolecular Crowding on the Conformational Ensembles of Disordered Proteins","volume":"4","author":"Qin","year":"2013","journal-title":"J. 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