five

Additional file 1 of High-throughput quantification of protein structural change reveals potential mechanisms of temperature adaptation in Mytilus mussels

收藏
DataCite Commons2020-08-25 更新2024-07-28 收录
下载链接:
https://springernature.figshare.com/articles/Additional_file_1_of_High-throughput_quantification_of_protein_structural_change_reveals_potential_mechanisms_of_temperature_adaptation_in_Mytilus_mussels/11853873/1
下载链接
链接失效反馈
官方服务:
资源简介:
Additional file 1: Figure S1. All unique proteins QMEAN >-5 M. galloprovincialis. Figure S2. All unique proteins QMEAN >-5 M. trossulus. Figure S3. All unique orthologs QMEAN >-5. Figure S4. Over-representation of M. galloprovincialis protein ontologies. Figure S5. Spearman rank correlation between the number of hydrogen bonds and salt bridges per amino acid among Mytilus proteins. Figure S6. Amino acid composition all unique proteins M. galloprovincialis. Figure S7. Amino acid composition all unique proteins M. trossulus. Figure S8. Chi square tests of independence comparing amino acid use in different sets of Mytilus proteins. Figure S9. Spearman rank order correlation between residue hydrophobicity or residue volume and deviation in amino acid use in M. galloprovincialis relative to M. trossulus for different sets of proteins.
提供机构:
figshare
创建时间:
2020-02-14
二维码
社区交流群
二维码
科研交流群
商业服务