Establishing knowledge on the sequence arrangement pattern of nucleated protein folding.
The heat-tolerance mechanisms of (hyper)thermophilic proteins provide a unique opportunity to investigate the unsolved protein folding problem. In an attempt to determine whether the interval between residues in sequence might play a role in determining thermostability, we constructed a sequence int...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2017-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC5342263?pdf=render |
| _version_ | 1819291487350816768 |
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| author | Fei Leng Chao Xu Xia-Yu Xia Xian-Ming Pan |
| author_facet | Fei Leng Chao Xu Xia-Yu Xia Xian-Ming Pan |
| author_sort | Fei Leng |
| collection | DOAJ |
| description | The heat-tolerance mechanisms of (hyper)thermophilic proteins provide a unique opportunity to investigate the unsolved protein folding problem. In an attempt to determine whether the interval between residues in sequence might play a role in determining thermostability, we constructed a sequence interval-dependent value function to calculate the residue pair frequency. Additionally, we identified a new sequence arrangement pattern, where like-charged residues tend to be adjacently assembled, while unlike-charged residues are distributed over longer intervals, using statistical analysis of a large sequence database. This finding indicated that increasing the intervals between unlike-charged residues can increase protein thermostability, with the arrangement patterns of these charged residues serving as thermodynamically favorable nucleation points for protein folding. Additionally, we identified that the residue pairs K-E, R-E, L-V and V-V involving long sequence intervals play important roles involving increased protein thermostability. This work demonstrated a novel approach for considering sequence intervals as keys to understanding protein folding. Our findings of novel relationships between residue arrangement and protein thermostability can be used in industry and academia to aid the design of thermostable proteins. |
| first_indexed | 2024-12-24T03:39:25Z |
| format | Article |
| id | doaj.art-92f44d793713421788ee153202a5495b |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-24T03:39:25Z |
| publishDate | 2017-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-92f44d793713421788ee153202a5495b2022-12-21T17:16:58ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01123e017358310.1371/journal.pone.0173583Establishing knowledge on the sequence arrangement pattern of nucleated protein folding.Fei LengChao XuXia-Yu XiaXian-Ming PanThe heat-tolerance mechanisms of (hyper)thermophilic proteins provide a unique opportunity to investigate the unsolved protein folding problem. In an attempt to determine whether the interval between residues in sequence might play a role in determining thermostability, we constructed a sequence interval-dependent value function to calculate the residue pair frequency. Additionally, we identified a new sequence arrangement pattern, where like-charged residues tend to be adjacently assembled, while unlike-charged residues are distributed over longer intervals, using statistical analysis of a large sequence database. This finding indicated that increasing the intervals between unlike-charged residues can increase protein thermostability, with the arrangement patterns of these charged residues serving as thermodynamically favorable nucleation points for protein folding. Additionally, we identified that the residue pairs K-E, R-E, L-V and V-V involving long sequence intervals play important roles involving increased protein thermostability. This work demonstrated a novel approach for considering sequence intervals as keys to understanding protein folding. Our findings of novel relationships between residue arrangement and protein thermostability can be used in industry and academia to aid the design of thermostable proteins.http://europepmc.org/articles/PMC5342263?pdf=render |
| spellingShingle | Fei Leng Chao Xu Xia-Yu Xia Xian-Ming Pan Establishing knowledge on the sequence arrangement pattern of nucleated protein folding. PLoS ONE |
| title | Establishing knowledge on the sequence arrangement pattern of nucleated protein folding. |
| title_full | Establishing knowledge on the sequence arrangement pattern of nucleated protein folding. |
| title_fullStr | Establishing knowledge on the sequence arrangement pattern of nucleated protein folding. |
| title_full_unstemmed | Establishing knowledge on the sequence arrangement pattern of nucleated protein folding. |
| title_short | Establishing knowledge on the sequence arrangement pattern of nucleated protein folding. |
| title_sort | establishing knowledge on the sequence arrangement pattern of nucleated protein folding |
| url | http://europepmc.org/articles/PMC5342263?pdf=render |
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