<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Adachi K</submitter><funding>NIDDK NIH HHS</funding><funding>NHLBI NIH HHS</funding><pagination>137-44</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2636675</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>481(2)</volume><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</pubmed_abstract><journal>Archives of biochemistry and biophysics</journal><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.</pubmed_title><pmcid>PMC2636675</pmcid><funding_grant_id>P60 HL038632-15S10002</funding_grant_id><funding_grant_id>R01 DK061692</funding_grant_id><funding_grant_id>U54 HL070596-050002</funding_grant_id><funding_grant_id>U54 HL070596</funding_grant_id><funding_grant_id>R01 HL069256</funding_grant_id><funding_grant_id>R56 DK061692</funding_grant_id><pubmed_authors>Surrey S</pubmed_authors><pubmed_authors>Adachi K</pubmed_authors><pubmed_authors>Asakura T</pubmed_authors><pubmed_authors>Ding M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Relationship between beta4 hydrogen bond and beta6 hydrophobic interactions during aggregate, fiber or crystal formation in oversaturated solutions of hemoglobin A and S.</name><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</description><dates><release>2009-01-01T00:00:00Z</release><publication>2009 Jan</publication><modification>2025-04-25T20:52:10.395Z</modification><creation>2019-03-27T00:20:36Z</creation></dates><accession>S-EPMC2636675</accession><cross_references><pubmed>19022217</pubmed><doi>10.1016/j.abb.2008.11.006</doi></cross_references></HashMap>