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ABSTRACT:
SUBMITTER: Reguera J
PROVIDER: S-EPMC365688 | biostudies-literature | 2004 Mar
REPOSITORIES: biostudies-literature
Reguera Juan J Carreira Aura A Riolobos Laura L Almendral José María JM Mateu Mauricio G MG
Proceedings of the National Academy of Sciences of the United States of America 20040223 9
Twenty-eight amino acid residues involved in most noncovalent interactions between trimeric protein subunits in the capsid of the parvovirus minute virus of mice were truncated individually to alanine, and the effects on capsid assembly, thermostability, and conformation were analyzed. Only seven side chains were essential for protein subunit recognition. These side chains virtually corresponded with those that either buried a large hydrophobic surface on trimer association or formed buried inte ...[more]