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: 1034
Function: getPubMedXML
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3152
Function: GetPubMedArticleOutput_2016
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
Structural features of a class of chromatin peptides are studied in the aim of understanding their mechanism of action. They have been reported as a family of small acidic peptides that can affect cell proliferation and RNA transcription. Mass spectrometry analysis has suggested some molecular models of possible sequences that might be present in this group of peptides. These sequences have been synthesised and their chromatographic and electrophoretic behaviour is compared with that obtained from peptides extracted from pea bud chromatin. In this way electric charge and hydrophilic properties of the native peptides are evaluated. On the basis of these data and those obtained from further mass spectrum analysis new models for native peptides are proposed.
Download full-text PDF |
Source |
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http://dx.doi.org/10.1023/a:1006813814125 | DOI Listing |
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