{"type":"journal_article","extern":"1","date_created":"2024-10-08T12:46:41Z","intvolume":"        13","publication_identifier":{"issn":["2045-2322"]},"has_accepted_license":"1","quality_controlled":"1","oa":1,"volume":13,"oa_version":"Published Version","doi":"10.1038/s41598-023-32821-z","main_file_link":[{"url":"https://doi.org/10.1038/s41598-023-32821-z","open_access":"1"}],"day":"13","publication":"Scientific Reports","publisher":"Springer Nature","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","year":"2023","tmp":{"image":"/images/cc_by.png","short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode"},"article_number":"6094","citation":{"ama":"Bronstein AM, Marx A. Water stabilizes an alternate turn conformation in horse heart myoglobin. <i>Scientific Reports</i>. 2023;13. doi:<a href=\"https://doi.org/10.1038/s41598-023-32821-z\">10.1038/s41598-023-32821-z</a>","short":"A.M. Bronstein, A. Marx, Scientific Reports 13 (2023).","chicago":"Bronstein, Alex M., and Ailie Marx. “Water Stabilizes an Alternate Turn Conformation in Horse Heart Myoglobin.” <i>Scientific Reports</i>. Springer Nature, 2023. <a href=\"https://doi.org/10.1038/s41598-023-32821-z\">https://doi.org/10.1038/s41598-023-32821-z</a>.","ista":"Bronstein AM, Marx A. 2023. Water stabilizes an alternate turn conformation in horse heart myoglobin. Scientific Reports. 13, 6094.","ieee":"A. M. Bronstein and A. Marx, “Water stabilizes an alternate turn conformation in horse heart myoglobin,” <i>Scientific Reports</i>, vol. 13. Springer Nature, 2023.","apa":"Bronstein, A. M., &#38; Marx, A. (2023). Water stabilizes an alternate turn conformation in horse heart myoglobin. <i>Scientific Reports</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41598-023-32821-z\">https://doi.org/10.1038/s41598-023-32821-z</a>","mla":"Bronstein, Alex M., and Ailie Marx. “Water Stabilizes an Alternate Turn Conformation in Horse Heart Myoglobin.” <i>Scientific Reports</i>, vol. 13, 6094, Springer Nature, 2023, doi:<a href=\"https://doi.org/10.1038/s41598-023-32821-z\">10.1038/s41598-023-32821-z</a>."},"date_published":"2023-04-13T00:00:00Z","status":"public","publication_status":"published","month":"04","article_type":"original","language":[{"iso":"eng"}],"author":[{"first_name":"Alexander","orcid":"0000-0001-9699-8730","last_name":"Bronstein","full_name":"Bronstein, Alexander","id":"58f3726e-7cba-11ef-ad8b-e6e8cb3904e6"},{"first_name":"Ailie","last_name":"Marx","full_name":"Marx, Ailie"}],"external_id":{"pmid":["37055458"]},"abstract":[{"text":"Comparison of myoglobin structures reveals that protein isolated from horse heart consistently adopts an alternate turn conformation in comparison to its homologues. Analysis of hundreds of high-resolution structures discounts crystallization conditions or the surrounding amino acid protein environment as explaining this difference, that is also not captured by the AlphaFold prediction. Rather, a water molecule is identified as stabilizing the conformation in the horse heart structure, which immediately reverts to the whale conformation in molecular dynamics simulations excluding that structural water.","lang":"eng"}],"_id":"18207","date_updated":"2024-10-09T10:39:26Z","article_processing_charge":"No","pmid":1,"title":"Water stabilizes an alternate turn conformation in horse heart myoglobin"}