tag:blogger.com,1999:blog-5834252248412211498.post653220193814249147..comments2023-10-02T19:15:59.038+10:00Comments on BIPH3001-Frontiers in Biophysics 2010: Allostery helps deliver oxygen to our tissuesMitch Ghttp://www.blogger.com/profile/12435777631824415803noreply@blogger.comBlogger2125tag:blogger.com,1999:blog-5834252248412211498.post-22536642638533679412010-09-21T23:37:09.749+10:002010-09-21T23:37:09.749+10:00It seemed weird to me that Nelson feigned suprise ...It seemed weird to me that Nelson feigned suprise that the binding of a molecule at one site in the protein can affect a spatially distant site. <br />I have two main reasons for this. Firstly the existence of long range effects such as London dispersion forces etc, electron transfer can also be across long distances in a protein. Secondly a protein is made of an amino acid chain, i.e. pulling on one end will move the other. Furthermore the chain is linked in a number of different ways as the protein folds. This would only increase the effect felt at one end of the protein when the other is dirupted.Heatherhttps://www.blogger.com/profile/13167610447846122237noreply@blogger.comtag:blogger.com,1999:blog-5834252248412211498.post-19076435661927167752010-09-21T22:28:04.856+10:002010-09-21T22:28:04.856+10:00Yeah, I understood that to be the case too. I thin...Yeah, I understood that to be the case too. I think a higher partial pressure of CO2 causes the local pH to increase (as H20+CO2<->2H+ + CO3(2-)), which in turn effects the binding between O2 and haemoglobin. However, I imagine it would be difficult to separately measure experimentally the effect of the change in pH and the effect of the change in CO2 concentration on the binding of O2 to haemoglobin.Mitch Ghttps://www.blogger.com/profile/12435777631824415803noreply@blogger.com