{"id":903,"date":"2018-09-03T00:30:22","date_gmt":"2018-09-02T23:30:22","guid":{"rendered":"https:\/\/www.nanoworld.com\/blog\/?p=903"},"modified":"2023-04-18T12:59:41","modified_gmt":"2023-04-18T11:59:41","slug":"mussel-adhesion-is-dictated-by-time-regulated-secretion-and-molecular-conformation-of-mussel-adhesive-proteins","status":"publish","type":"post","link":"https:\/\/www.nanoworld.com\/blog\/mussel-adhesion-is-dictated-by-time-regulated-secretion-and-molecular-conformation-of-mussel-adhesive-proteins\/","title":{"rendered":"Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins"},"content":{"rendered":"

We have a month with “R” again and the shellfish season has started in the Northern Hemisphere. So we’d like to share the Nature Communications article by Petrone et. al “Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins<\/a>” with you.
\nA NanoWorld Pointprobe\u00ae<\/strong> NCSTR<\/a> AFM probe was used for the AFM images in this paper. This AFM probe is designed to give extra stability and accuracy during soft tapping mode imaging in order to produce higher quality AFM images while minimizing sample damage.<\/p>\n

\"Supplementary<\/a>
Supplementary Figure 16 from Petrone et. al “Mussel adhesion is dictated by time-regulated<\/a>
secretion and molecular conformation of mussel adhesive proteins”:
Atomic Force Microscopy (AFM) of mussel adhesive proteins on mica. AFM images of dry Pvfp-3\u03b1 and Pvfp-5\u03b2 adsorbed from 0.02 mg ml-1 solution in 5% acetic acid and 0.25 MO3 on mica. After 20 min adsorption, the mica surfaces were washed with protein -free buffer, and the AFM images show the homogenous distribution of the resulting adsorbed proteins. The height profiles for both proteins are shown in the graphs below, corresponding to the dotted red and blue lines in the respective AFM images (see black arrows).<\/figcaption><\/figure>\n

Luigi Petrone, Akshita Kumar, Clarinda N. Sutanto, Navinkumar J. Patil, Srinivasaraghavan Kannan, Alagappan Palaniappan, Shahrouz Amini, Bruno Zappone, Chandra Verma, Ali Miserez
\nMussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins<\/strong>
\nNature Communications volume 6, Article number: 8737 (2015)
\nDOI https:\/\/doi.org\/10.1038\/ncomms9737<\/a><\/p>\n

Please follow this external link for the full article: https:\/\/rdcu.be\/5vcI<\/a><\/p>\n

\n

The article <\/span><\/span>by Petrone, L.<\/span>et al. “<\/span>Mussel adhesion is dictated by time-regulated <\/span>secretion and molecular conformation of mussel adhesive proteins” <\/span>is licensed under a Creative Commons Attribution 4.0 <\/span>International License. The images or other third party material in this <\/span>article are included in the article\u2019s Creative Commons license, unless indicated otherwise <\/span>in the credit line; if the material is not included under the Creative Commons license, <\/span>users will need to obtain permission from the license holder to reproduce the m<\/span>aterial. To view a copy of this license, visit http:\/\/creativecommons.org\/licenses\/by\/4.0\/<\/p>\n<\/div>\n","protected":false},"excerpt":{"rendered":"

We have a month with “R” again and the shellfish season has started in the Northern Hemisphere. So we’d like to share the Nature Communications article by Petrone et. al “Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins” with you. A NanoWorld Pointprobe\u00ae NCSTR AFM probe was used for … Continue reading Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins<\/span><\/a><\/p>\n","protected":false},"author":3,"featured_media":0,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[3],"tags":[164,11,8,10,17,93,48,90,91,88,76,38,16,89,14,13,12,92,21],"class_list":["post-903","post","type-post","status-publish","format-standard","hentry","category-news","tag-adhesion","tag-afm-cantilever","tag-afm-probe","tag-afm-tips","tag-atomic-force-microscopy","tag-biology","tag-biology-afm-probes","tag-biomaterials-proteins","tag-biophysical-chemistry","tag-ncstr","tag-non-contact-afm","tag-pointprobe","tag-scanning-probe-microscopy","tag-soft-tapping-mode","tag-spm-cantilevers","tag-spm-probes","tag-spm-tips","tag-structural-biology","tag-tapping-mode"],"_links":{"self":[{"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/posts\/903","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/comments?post=903"}],"version-history":[{"count":12,"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/posts\/903\/revisions"}],"predecessor-version":[{"id":916,"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/posts\/903\/revisions\/916"}],"wp:attachment":[{"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/media?parent=903"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/categories?post=903"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.nanoworld.com\/blog\/wp-json\/wp\/v2\/tags?post=903"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}