<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>3(5)</volume><submitter>Rasheed F</submitter><funding>Tr?d och gr?dor f?r framtid, Sveriges Lantbruksuniversitet</funding><funding>VINNOVA</funding><funding>Vetenskapsr?det</funding><pubmed_abstract>A combination of genotype, cultivation environment, and protein separation procedure was used to modify the nanoscale morphology, polymerization, and chemical structure of glutenin proteins from wheat. A low-polymerized glutenin starting material was the key to protein-protein interactions mainly via SS cross-links during film formation, resulting in extended β-sheet structures and propensity toward the formation of nanoscale morphologies at molecular level. The properties of glutenin bioplastic films were enhanced by the selection of a genotype with a high number of cysteine residues in its chemical structure and cultivation environment with a short grain maturation period, both contributing positively to gluten strength. Thus, a combination of factors affected the structure of glutenins </pubmed_abstract><journal>ACS omega</journal><pagination>5584-5592</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6045469</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Unraveling the Structural Puzzle of the Giant Glutenin Polymer-An Interplay between Protein Polymerization, Nanomorphology, and Functional Properties in Bioplastic Films.</pubmed_title><pmcid>PMC6045469</pmcid><pubmed_authors>Plivelic TS</pubmed_authors><pubmed_authors>Hedenqvist MS</pubmed_authors><pubmed_authors>Kuktaite R</pubmed_authors><pubmed_authors>Johansson E</pubmed_authors><pubmed_authors>Rasheed F</pubmed_authors></additional><is_claimable>false</is_claimable><name>Unraveling the Structural Puzzle of the Giant Glutenin Polymer-An Interplay between Protein Polymerization, Nanomorphology, and Functional Properties in Bioplastic Films.</name><description>A combination of genotype, cultivation environment, and protein separation procedure was used to modify the nanoscale morphology, polymerization, and chemical structure of glutenin proteins from wheat. A low-polymerized glutenin starting material was the key to protein-protein interactions mainly via SS cross-links during film formation, resulting in extended β-sheet structures and propensity toward the formation of nanoscale morphologies at molecular level. The properties of glutenin bioplastic films were enhanced by the selection of a genotype with a high number of cysteine residues in its chemical structure and cultivation environment with a short grain maturation period, both contributing positively to gluten strength. Thus, a combination of factors affected the structure of glutenins </description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 May</publication><modification>2025-04-19T07:53:54.026Z</modification><creation>2019-03-26T23:47:03Z</creation></dates><accession>S-EPMC6045469</accession><cross_references><pubmed>30023922</pubmed><doi>10.1021/acsomega.7b02081</doi></cross_references></HashMap>