Talk:Beta sheet

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Super-Secondary Structure?

Being that β sheets are composed of β strands, themselves already secondary structures, could not β sheets be considered supersecondary structure? —Raymond Keller (talk) 00:54, 6 November 2011 (UTC)[reply]

It is indeed a moot point. But a truly isolated β strand is then not really secondary structure, so usually it is the sheet that is talked about, altho it would be the strand if annotating along the sequence. I'd be fine with adding sheets to a discussion of supersecondary structure, but not with omitting it from secondary structure. - Dcrjsr (talk) 16:22, 4 July 2012 (UTC)[reply]

I've reconsidered, and think this is only C class for Biophysics -- a few of the figures are very poor, and the coverage is still rather spotty. Dcrjsr (talk) 00:12, 14 July 2012 (UTC)[reply]

Update to Dynamic features

This update has been challenged as COI please weigh in.

Beta-sheets in proteins are thought to carry out low-frequency accordion-like motion as observed by the Raman spectroscopy^[1] and analyzed with the quasi-continuum model.^[2]

The beta-barrel protein GFP has been shown by neutron scattering to undergo collective motions of adjacent chains at ~1 THz.^[3] These motions are thought reflect local rigidity within proteins, revealing beta structures to be generically more rigid than alpha or disordered proteins.^[4]^[5]

above comment by — Preceding unsigned comment added by Jon33dn (talk • contribs) 00:24, 21 February 2015‎ (UTC)[reply]

References

^ Painter PC, Mosher LE, Rhoads C (July 1982). "Low-frequency modes in the Raman spectra of proteins". Biopolymers. 21 (7): 1469–72. doi:10.1002/bip.360210715. PMID 7115900.{{cite journal}}: CS1 maint: multiple names: authors list (link)
^ Chou KC (August 1985). "Low-frequency motions in protein molecules. Beta-sheet and beta-barrel". Biophys. J. 48 (2): 289–97. doi:10.1016/S0006-3495(85)83782-6. PMC 1329320. PMID 4052563.
^ Nickels JD, Perticaroli S, O'Neill H, Zhang Q, Ehlers G, Sokolov AP (2013). "Coherent neutron scattering and collective dynamics in the protein, GFP". Biophys. J. 105 (9): 2182–7. doi:10.1016/j.bpj.2013.09.029. PMC 3824694. PMID 24209864.
^ Perticaroli S, Nickels JD, Ehlers G, O'Neill H, Zhang Q, Sokolov AP (2013). "Secondary structure and rigidity in model proteins". Soft Matter. 9 (40): 9548. doi:10.1039/C3SM50807B.
^ Perticaroli S, Nickels JD, Ehlers G, Sokolov AP (2014). "Rigidity, secondary structure, and the universality of the boson peak in proteins". Biophys. J. 106 (12): 2667–74. doi:10.1016/j.bpj.2014.05.009. PMID 24940784.

If you read our content policies, WP:OR and WP:NPOV, and our guidelines for sources, WP:RS and WP:MEDRS, you will see that all of them strongly urge editors to use secondary sources. There are many many reasons why this is best practice. What is your reason for wanting to use primary sources at all, and these primary sources in particular? Also, based on your editing behavior, Boghog warned you that you may have a COI (as we consider WP:COI) and warned you to be careful to avoid WP:SELFCITE. So - are you citing your own research, or not? Please answer those three questions. Thanks.Jytdog (talk) 00:31, 21 February 2015 (UTC)[reply]

Assessment comment

The comment(s) below were originally left at Talk:Beta sheet/Comments, and are posted here for posterity. Following several discussions in past years, these subpages are now deprecated. The comments may be irrelevant or outdated; if so, please feel free to remove this section.

202.40.139.165 07:57, 15 March 2007 (UTC)the description under the diagram of beta sheet is wrong, the one on the left should be parallel and the one on the right should be antiparallel instead.202.40.139.165 07:57, 15 March 2007 (UTC) Can one beta sheet be more compressed than another or is this structural type consisted between one protein and another? Smelias1 (talk) 01:02, 4 November 2008 (UTC)[reply]

Last edited at 01:02, 4 November 2008 (UTC). Substituted at 09:32, 29 April 2016 (UTC)

[pmid7115900-1] Painter PC, Mosher LE, Rhoads C (July 1982). "Low-frequency modes in the Raman spectra of proteins". Biopolymers. 21 (7): 1469–72. doi:10.1002/bip.360210715. PMID 7115900.{{cite journal}}: CS1 maint: multiple names: authors list (link)

[pmid4052563-2] Chou KC (August 1985). "Low-frequency motions in protein molecules. Beta-sheet and beta-barrel". Biophys. J. 48 (2): 289–97. doi:10.1016/S0006-3495(85)83782-6. PMC 1329320. PMID 4052563.

[pmid24209864-3] Nickels JD, Perticaroli S, O'Neill H, Zhang Q, Ehlers G, Sokolov AP (2013). "Coherent neutron scattering and collective dynamics in the protein, GFP". Biophys. J. 105 (9): 2182–7. doi:10.1016/j.bpj.2013.09.029. PMC 3824694. PMID 24209864.

[4] Perticaroli S, Nickels JD, Ehlers G, O'Neill H, Zhang Q, Sokolov AP (2013). "Secondary structure and rigidity in model proteins". Soft Matter. 9 (40): 9548. doi:10.1039/C3SM50807B.

[pmid24940784-5] Perticaroli S, Nickels JD, Ehlers G, Sokolov AP (2014). "Rigidity, secondary structure, and the universality of the boson peak in proteins". Biophys. J. 106 (12): 2667–74. doi:10.1016/j.bpj.2014.05.009. PMID 24940784.

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