Ribonuclease T1
Appearance
Ribonuclease T1 | |||||||||
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ExPASy NiceZyme view | | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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Ribonuclease T1 | |||||||
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UniProt P00651 | | ||||||
Other data | |||||||
EC number | 4.6.1.24 | ||||||
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Ribonuclease T1 (
RNase A, ribonuclease T1 has been popular for folding studies.[2]
Structurally, ribonuclease T1 is a small α+β protein (104 amino acids) with a four-stranded, antiparallel beta sheet covering a long alpha helix (almost five turns). RNase T1 has two disulfide bonds, Cys2-Cys10 and Cys6-Cys103, of which the latter contributes more to its folding stability;[3] complete reduction of both disulfides usually unfolds the protein, although its folding can be rescued with high salt concentrations.[4]
RNase T1 also has four prolines, two of which (Pro39 and Pro55) have cis isomers of their X-Pro peptide bonds. Nonnative isomers of these prolines can retard conformational folding dramatically,[5] folding on a characteristic time scale of 7,000 seconds (almost two hours) at 10 °C and pH 5.[6]
References
- PMID 9047372.
- ^ Pace CN, Heinemann U, Hahn U, Saenger W (1991). "Ribonuclease T1: Structure, Function, and Stability". .
- ^
Pace CN, Grimsley GR, Thomson JA, Barnett BJ (1988). "Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds". PMID 2457027.
- ^ Oobatake M, Takahashi S, Ooi T (1979). "Conformational stability of ribonuclease T1. II. Salt-induced renaturation". Journal of Biochemistry. 86: 65–70.
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Mayr LM, Odefey CO, Schutkowski M, Schmid FX (1996). "Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique". PMID 8611546.
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Mullins LS, Pace CN, Raushel FM (1997). "Conformational stability of ribonuclease T1 measured by hydrogen-deuterium exchange". PMID 9232639.
External links
- Ribonuclease+T1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)