Severity: Warning
Message: file_get_contents(https://...@gmail.com&api_key=61f08fa0b96a73de8c900d749fcb997acc09&a=1): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
Filename: helpers/my_audit_helper.php
Line Number: 197
Backtrace:
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 197
Function: file_get_contents
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 271
Function: simplexml_load_file_from_url
File: /var/www/html/application/helpers/my_audit_helper.php
Line: 3165
Function: getPubMedXML
File: /var/www/html/application/controllers/Detail.php
Line: 597
Function: pubMedSearch_Global
File: /var/www/html/application/controllers/Detail.php
Line: 511
Function: pubMedGetRelatedKeyword
File: /var/www/html/index.php
Line: 317
Function: require_once
98%
921
2 minutes
20
The effect of external electric field (EEF) of 5.14, 25.70, and 51.40 MV/cm upon Cys-Asn-Ser, Glu-Arg-Leu, Glu-Cys-Glc, Ser-Asp-Leu, Ser-Glu-Met tripeptide inner salts was simulated involving HyperChem 8.0 software together with the AM1 method for optimization of the molecules' conformation. The reaction to EEF is diverse and specific to particular peptides. EEF stimulated an increase in the positive charge density on the hydrogen atoms of the N(+)H3, peptide bond NH, NH2, and COOH groups as well decrease in the negative charge density on the oxygen atoms of the peptide bond carbonyl groups. Thus, EEF could control behavior and action of tripeptides, such as an increase in their catalytic activity.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1007/s00726-015-1971-8 | DOI Listing |