Data from: Peptide sequences from the first Castoroides ohioensis skull and the utility of old museum collections for paleoproteomics

Vertebrate fossils have been collected for hundreds years and are stored in museum collections around the world. These remains provide a readily available resource to search for preserved proteins; however, the vast majority of paleoproteomic studies have focused on relatively recently collected bones with a well-known handling history. Here, we characterize proteins from the nasal turbinates of the first Castoroides ohioensis skull ever discovered. Collected in 1845, this is the oldest museum curated specimen characterized using paleoproteomic tools. Our mass spectrometry analysis detected many collagen I peptides, a peptide from hemoglobin beta, and in vivo and diagenetic post-translational modifications. Additionally, the identified collagen I sequences provide enough resolution to place C. ohioensis within Rodentia. This study illustrates the utility of archived museum specimens for both the recovery of preserved proteins and phylogenetic analyses.脊椎动物化石的采集已有数百年历史，且被收藏于全球各地的博物馆馆藏之中。这些化石遗骸为搜寻保存态蛋白质提供了易得的研究资源；然而，绝大多数古蛋白质组学（Paleoproteomics）研究均聚焦于采集时间较近、经手历史明确的骨骼标本。本研究首次对有史以来发现的首具俄亥俄巨河狸（Castoroides ohioensis）头骨的鼻甲（nasal turbinates）开展蛋白质特征分析。该标本采集于1845年，是目前利用古蛋白质组学工具完成特征分析的最古老博物馆馆藏标本。本研究的质谱分析法（Mass Spectrometry）检测到多种I型胶原蛋白（Collagen I）肽段、一条β-珠蛋白（Hemoglobin beta）肽段，以及体内成因与成岩成因的翻译后修饰（Post-translational Modifications）。此外，所鉴定出的I型胶原蛋白序列具备足够的系统发育分辨率，可将俄亥俄巨河狸（C. ohioensis）归入啮齿目（Rodentia）。本研究证实了馆藏博物馆标本在保存态蛋白质提取与系统发育分析两方面的应用价值。