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
Atomic force microscopy (AFM) makes it possible to obtain images at nanometric resolution, and to accomplish the manipulation and physical characterization of specimens, including the determination of their mechanical and electrostatic properties. AFM has an ample range of applications, from materials science to biology. The specimen, supported on a solid surface, can be imaged and manipulated while working in air, ultra-high vacuum or, most importantly for virus studies, in liquid. The adaptability of AFM is also favored by the large variety of specimens of very different sizes that it can deal with, such as atoms, molecules, and molecular complexes including viruses and cells. AFM allows, in addition, the possibility to observe dynamics in real time. Indeed, AFM facilitates single molecule experiments enabling not only to see but also to touch the material under study (i.e., mechanical manipulations) and constitutes a fundamental source of information for materials characterization. In particular, the study of the mechanical properties of viruses and other biomolecular aggregates at the nanoscale is providing humongous information This helps to elaborate mechano-chemical structure/function models of complex protein aggregates, expanding and complementing the information obtained by other techniques.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1007/978-3-031-65187-8_9 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!