التفاصيل البيبلوغرافية
| العنوان: |
Probing the Energy Landscape of Spectrin R15 and R16 and the Effects of Non-native Interactions. |
| المؤلفون: |
da Silva FB; Department of Physics, São Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences, São José do Rio Preto, São Paulo15054-000, Brazil., Martins de Oliveira V; Department of Pharmaceutical Sciences, University of Maryland School of Pharmacy, Baltimore, Maryland21201, United States., de Oliveira Junior AB; Center for Theoretical Biological Physics, Rice University, Houston, Texas77005-1892, United States., Contessoto VG; Center for Theoretical Biological Physics, Rice University, Houston, Texas77005-1892, United States., Leite VBP; Department of Physics, São Paulo State University (UNESP), Institute of Biosciences, Humanities and Exact Sciences, São José do Rio Preto, São Paulo15054-000, Brazil. |
| المصدر: |
The journal of physical chemistry. B [J Phys Chem B] 2023 Feb 16; Vol. 127 (6), pp. 1291-1300. Date of Electronic Publication: 2023 Feb 01. |
| نوع المنشور: |
Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: |
English |
| بيانات الدورية: |
Publisher: American Chemical Society Country of Publication: United States NLM ID: 101157530 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5207 (Electronic) Linking ISSN: 15205207 NLM ISO Abbreviation: J Phys Chem B Subsets: MEDLINE |
| أسماء مطبوعة: |
Original Publication: Washington, D.C. : American Chemical Society, c1997- |
| مواضيع طبية MeSH: |
Spectrin*/chemistry , Protein Folding*, Kinetics ; Thermodynamics ; Physical Phenomena |
| مستخلص: |
Understanding the details of a protein folding mechanism can be a challenging and complex task. One system with an interesting folding behavior is the α-spectrin domain, where the R15 folds three-orders of magnitude faster than its homologues R16 and R17, despite having similar structures. The molecular origins that explain these folding rate differences remain unclear, but our previous work revealed that a combined effect produced by non-native interactions could be a reasonable cause for these differences. In this study, we explore further the folding process by identifying the molecular paths, metastable states, and the collective motions that lead these unfolded proteins to their native state conformation. Our results uncovered the differences between the folding pathways for the wild-type R15 and R16 and an R16 mutant. The metastable ensembles that speed down the folding were identified using an energy landscape visualization method (ELViM). These ensembles correspond to similar experimentally reported configurations. Our observations indicate that the non-native interactions are also associated with secondary structure misdocking. This computational methodology can be used as a fast, straightforward protocol for shedding light on systems with unclear folding or conformational traps. |
| المشرفين على المادة: |
12634-43-4 (Spectrin) |
| تواريخ الأحداث: |
Date Created: 20230201 Date Completed: 20230217 Latest Revision: 20230308 |
| رمز التحديث: |
20231215 |
| DOI: |
10.1021/acs.jpcb.2c06178 |
| PMID: |
36723393 |
| قاعدة البيانات: |
MEDLINE |
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