Severity: Warning
Message: file_get_contents(https://...@pubfacts.com&api_key=b8daa3ad693db53b1410957c26c9a51b4908&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 176
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 176
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 250
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3122
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 575
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 489
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 316
Function: require_once
Mutations, which can alter amino acid constitution, contribute greatly to protein evolution. However, little is reported of their pattern during protein structural evolution. We investigated the distribution of non-synonymous single nucleotide polymorphisms (nsSNPs) and insertions/deletions (indels) along mammal and fruit fly proteins. We found the nsSNPs (and d(N)) and indels increased in protein boundary regions, and this pattern is inversely correlated with the distribution of protein domain density. Additionally, synonymous substitutions (and d(S)) are reduced in 5' and 3' regions, indicating more variable protein boundaries, compared with central interior. All evidence suggests that the inner part of coding sequences (CDSs) is comparatively conserved, whereas the 5' and 3' regions, with higher evolution rates, are more variable. We assumed that due to greater frequencies of nsSNPs and indels in adaptive regions of CDSs it could be easier to ultimately alter, gain, or lose amino acids, thus becoming the front line of protein evolution.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1016/j.ygeno.2008.09.009 | DOI Listing |
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