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FEBS Letters
Article . 1988 . Peer-reviewed
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FEBS Letters
Article . 1988
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The tertiary structure of Aspergillus saitoi minor ribonuclease (Ms) predicted from the structure of RNase T1

Authors: Rainer Flogel; Piotr Zielenkiewicz; Wolfram Saenger;

The tertiary structure of Aspergillus saitoi minor ribonuclease (Ms) predicted from the structure of RNase T1

Abstract

Ribonuclease Ms from Aspergillus saitoi is a small acidic protein (11 714 Da) containing 106 amino acids of known sequence. Unlike other enzymes belonging to the RNase T1 family this ribonuclease is base‐unspecific. Using interactive computer graphics and energy minimisation we predicted the structure of RNase Ms on the basis of sequence homology to RNase T1 of known structure. In this report the predicted structure of this protein is presented and characterised.

Keywords

Models, Molecular, Protein Conformation, Molecular Sequence Data, Hydrogen Bonding, (Aspergillus saitoi), Energy minimization, Computer graphics, Aspergillus, Ribonuclease Ms, Structure prediction, Endoribonucleases, Computer Simulation, Amino Acid Sequence, Ribonuclease T1

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    7
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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
7
Average
Average
Average
bronze
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Energy Research