SUBJECT: [ &NAME ] &NAME &NAME Wednesday 23rd April Dear All , &NAME &NAME from the &NAME will present a seminar to the &NAME group entitled : ' Solubility and protein-solvent interfaces of monomeric proteins ' DATE : 23rd April ( Wednesday ) TIME : 11.30am-12.30pm TRANSPORT : &NUM &NUM a.m. Tennis &NAME Road , in front of the new &NAME department &NUM &NUM a.m. &NAME ( roundabout ) and back after the talk . Can people who are planning on using the bus please email back to me , so that we have some idea of the numbers on the bus Also , as you know there is a &NAME talk at the &NAME on the 22nd April . There will also be a bus running to this talk , leaving &NAME / &NAME at &NUM 40am . ABSTRACT : &NAME is understood in the relationship between the sequence , structure and solubility of a protein . However , it is clear that the function of a protein is intimately related to its solubility , namely that structural proteins are insoluble while enzymes must have a very high solubility . Our inability to predict solubility presents practical difficulties , especially for &NAME &NAME Initiatives as up to &NUM of non-membrane proteins cannot be crystallised due to insolubility of the sample . Furthermore , it seems plausible that the mechanisms responsible for the formation of insoluble amyloid fibrils are similar to those at play in the formation of the random insoluble aggregates that form in inclusion bodies . It is clear that the hydrophobic ( or polar ) content of the surface of a protein plays a key role in its solubility . Given the collective behaviour of water , we hypothesise , that individual surface residues may not necessarily play a decisive role in dictating its solubility but that patches of residues may well do so . To examine this , we construct a score based on the average hydrophobic / polar content of surface patches of atoms ( or residues ) over a set of &NUM monomeric proteins . To see if the resulting distribution of scores is unusal we compare the distribution of scores for each protein with the scores from an equivalent randomised surface . We can also examine the variation of the score for each patch over homologous proteins . Here too we can compare the distribution of scores with scores generated from randomised sequences . In the first case , we find that the atomic patch score , have distributions with shorter tails than those generated from the randomised surfaces indicating that the surface atoms are arranging themselves so as to avoid extrema of hydrophobicity or hydrophilicity . Perhaps more interestingly , in the case of examining the hydrophobic patch score as it varys over sequences , we find that hydrophobic patches tend to be supressed , suggesting that surface residues can evolve in a collective fashion . We argue that this confirms our initial hypothesis , what its consequences are and some future research we can carry out . I hope to see many of you at the talk , Regards , &NAME subscribe or unsubscribe from &NAME by sending an email with title ' subscribe &NAME ' or ' unsubscribe &NAME ' to &EMAIL