Title : Investigation of a conserved stacking interaction in target site recognition by the U1A protein.

Pub. Date : 2002 Jan 15

PMID : 11788718






2 Functional Relationships(s)
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Protein Name
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1 Here we probe how mutation of Phe56 affects the kinetics of complex dissociation, the strength of the hydrogen bonds formed between U1A and the base that stacks with Phe56 (A6) and specific target site recognition. Hydrogen small nuclear ribonucleoprotein polypeptide A Homo sapiens
2 Simultaneous modification of residue 56 and A6 revealed energetic coupling between the aromatic group and the functional groups of A6 that hydrogen bond to U1A. Hydrogen small nuclear ribonucleoprotein polypeptide A Homo sapiens