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疏水相互作用对内向/外向跨膜转运蛋白构象变化的贡献。

The Contribution of Hydrophobic Interactions to Conformational Changes of Inward/Outward Transmembrane Transport Proteins.

作者信息

Roterman Irena, Stapor Katarzyna, Konieczny Leszek

机构信息

Department of Bioinformatics and Telemedicine, Jagiellonian University-Medical College Medyczna 7, 30-688 Kraków, Poland.

Department of Applied Informatics, Faculty of Automatic, Electronics and Computer Science, Silesian University of Technology, Akademicka 16, 44-100 Gliwice, Poland.

出版信息

Membranes (Basel). 2022 Nov 30;12(12):1212. doi: 10.3390/membranes12121212.

DOI:10.3390/membranes12121212
PMID:36557119
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9784565/
Abstract

Proteins transporting ions or other molecules across the membrane, whose proper concentration is required to maintain homeostasis, perform very sophisticated biological functions. The symport and antiport active transport can be performed only by the structures specially prepared for this purpose. In the present work, such structures in both In and Out conformations have been analyzed with respect to the hydrophobicity distribution using the FOD-M model. This allowed for identifying the role of individual protein chain fragments in the stabilization of the specific cell membrane environment as well as the contribution of hydrophobic interactions to the conformational changes between In/Out conformations.

摘要

负责跨膜转运离子或其他分子的蛋白质,其适当浓度对于维持体内平衡至关重要,它们执行着非常复杂的生物学功能。同向转运和反向转运的主动运输只能由为此专门准备的结构来完成。在本研究中,利用FOD-M模型对处于向内和向外构象的此类结构的疏水性分布进行了分析。这有助于确定蛋白质单链片段在特定细胞膜环境稳定中的作用,以及疏水相互作用对向内/向外构象之间构象变化的贡献。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/023a7f3c37fc/membranes-12-01212-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/54bbe26c7540/membranes-12-01212-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/2e577e55a16f/membranes-12-01212-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/3b0fd7d9c067/membranes-12-01212-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/acb63aa8bab8/membranes-12-01212-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/8bfa12a50875/membranes-12-01212-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/a4103d72a7b9/membranes-12-01212-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/01178d059525/membranes-12-01212-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/aca2edf6c728/membranes-12-01212-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/023a7f3c37fc/membranes-12-01212-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/54bbe26c7540/membranes-12-01212-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/2e577e55a16f/membranes-12-01212-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/3b0fd7d9c067/membranes-12-01212-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/acb63aa8bab8/membranes-12-01212-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/8bfa12a50875/membranes-12-01212-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/a4103d72a7b9/membranes-12-01212-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/01178d059525/membranes-12-01212-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/aca2edf6c728/membranes-12-01212-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e97c/9784565/023a7f3c37fc/membranes-12-01212-g009.jpg

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