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| | {{STRUCTURE_1rhl| PDB=1rhl | SCENE= }} | | {{STRUCTURE_1rhl| PDB=1rhl | SCENE= }} |
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| - | '''RIBONUCLEASE T1 COMPLEXED WITH 2'GMP/G23A MUTANT'''
| + | ===RIBONUCLEASE T1 COMPLEXED WITH 2'GMP/G23A MUTANT=== |
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| - | ==Overview==
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| - | Hydrogen-exchange rates were measured for RNase T1 and three variants with Ala --> Gly substitutions at a solvent-exposed (residue 21) and a buried (residue 23) position in the helix: A21G, G23A, and A21G + G23A. These results were used to measure the stabilities of the proteins. The hydrogen-exchange stabilities (DeltaG(HX)) for the most stable residues in each variant agree with the equilibrium conformational stability measured by urea denaturation (DeltaG(U)), if the effects of D(2)O and proline isomerization are included [Huyghues-Despointes, B. M. P., Scholtz, J. M., and Pace, C. N. (1999) Nat. Struct. Biol. 6, 210-212]. These residues also show similar changes in DeltaG(HX) upon Ala --> Gly mutations (DeltaDeltaG(HX)) as compared to equilibrium measurements (DeltaDeltaG(U)), indicating that the most stable residues are exchanging from the globally unfolded ensemble. Alanine is stabilizing compared to glycine by 1 kcal/mol at a solvent-exposed site 21 as seen by other methods for the RNase T1 protein and peptide helix [Myers, J. K., Pace, C. N., and Scholtz, J. M. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 3833-2837], while it is destabilizing at the buried site 23 by the same amount. For the A21G variant, only local NMR chemical shift perturbations are observed compared to RNase T1. For the G23A variant, large chemical shift changes are seen throughout the sequence, although X-ray crystal structures of the variant and RNase T1 are nearly superimposable. Ala --> Gly mutations in the helix of RNase T1 at both helical positions alter the native-state hydrogen-exchange stabilities of residues throughout the sequence.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10600109}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10600109 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10600109}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Endoribonuclease]] | | [[Category: Endoribonuclease]] |
| | [[Category: Ribonuclease]] | | [[Category: Ribonuclease]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:30:30 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:54:24 2008'' |
Revision as of 09:54, 28 July 2008
Template:STRUCTURE 1rhl
RIBONUCLEASE T1 COMPLEXED WITH 2'GMP/G23A MUTANT
Template:ABSTRACT PUBMED 10600109
About this Structure
1RHL is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.
Reference
Hydrogen-exchange stabilities of RNase T1 and variants with buried and solvent-exposed Ala --> Gly mutations in the helix., Huyghues-Despointes BM, Langhorst U, Steyaert J, Pace CN, Scholtz JM, Biochemistry. 1999 Dec 14;38(50):16481-90. PMID:10600109
Page seeded by OCA on Mon Jul 28 12:54:24 2008
