{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Adachi K"],"funding":["NIDDK NIH HHS","NHLBI NIH HHS"],"pagination":["137-44"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2636675"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["481(2)"],"pubmed_abstract":["Oversaturated deoxy-alpha(2)beta(2)(T4V) aggregated instantly without a delay time, which is in contrast to the delay time before the generation of fibers of deoxy-HbS and deoxy-alpha(2)beta(2)(E6V,D73H). Solubility of deoxy-alpha(2)beta(2)(T4V) was approximately 10-fold lower than that of deoxy-HbS and was similar to oxy- and deoxy-alpha(2)beta(2)(E6V,T4V). These results indicate that beta4Val in HbA in the oxy and deoxy forms with or without beta6Val facilitates hydrophobic interaction of the A-helix with the EF helix of adjacent molecules without forming a beta4/beta73 hydrogen bond. Deoxy-HbA generated crystals following aggregation as does HbC-Harlem(alpha(2)beta(2)(E6V,D73N)), while alpha(2)beta(2)(T4V) and alpha(2)beta(2)(D73H) as well as HbS, alpha(2)beta(2)(E6V,D73H) and alpha(2)b"],"journal":["Archives of biochemistry and biophysics"],"pubmed_title":["Relationship between beta4 hydrogen bond and beta6 hydrophobic interactions during aggregate, fiber or crystal formation in oversaturated solutions of hemoglobin A and S."],"pmcid":["PMC2636675"],"funding_grant_id":["P60 HL038632-15S10002","R01 DK061692","U54 HL070596-050002","U54 HL070596","R01 HL069256","R56 DK061692"],"pubmed_authors":["Surrey S","Adachi K","Asakura T","Ding M"],"additional_accession":[]},"is_claimable":false,"name":"Relationship between beta4 hydrogen bond and beta6 hydrophobic interactions during aggregate, fiber or crystal formation in oversaturated solutions of hemoglobin A and S.","description":"Oversaturated deoxy-alpha(2)beta(2)(T4V) aggregated instantly without a delay time, which is in contrast to the delay time before the generation of fibers of deoxy-HbS and deoxy-alpha(2)beta(2)(E6V,D73H). Solubility of deoxy-alpha(2)beta(2)(T4V) was approximately 10-fold lower than that of deoxy-HbS and was similar to oxy- and deoxy-alpha(2)beta(2)(E6V,T4V). These results indicate that beta4Val in HbA in the oxy and deoxy forms with or without beta6Val facilitates hydrophobic interaction of the A-helix with the EF helix of adjacent molecules without forming a beta4/beta73 hydrogen bond. Deoxy-HbA generated crystals following aggregation as does HbC-Harlem(alpha(2)beta(2)(E6V,D73N)), while alpha(2)beta(2)(T4V) and alpha(2)beta(2)(D73H) as well as HbS, alpha(2)beta(2)(E6V,D73H) and alpha(2)b","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Jan","modification":"2025-04-25T20:52:10.395Z","creation":"2019-03-27T00:20:36Z"},"accession":"S-EPMC2636675","cross_references":{"pubmed":["19022217"],"doi":["10.1016/j.abb.2008.11.006"]}}