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| - | [[Image:2rln.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2rln| PDB=2rln | SCENE= }} | | {{STRUCTURE_2rln| PDB=2rln | SCENE= }} |
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| - | '''THERMODYNAMIC AND STRUCTURAL CONSEQUENCES OF CHANGING A SULPHUR ATOM TO A METHYLENE GROUP IN THE M13NLE MUTATION IN RIBONUCLEASE S'''
| + | ===THERMODYNAMIC AND STRUCTURAL CONSEQUENCES OF CHANGING A SULPHUR ATOM TO A METHYLENE GROUP IN THE M13NLE MUTATION IN RIBONUCLEASE S=== |
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| - | ==Overview==
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| - | Two fragments of pancreatic ribonuclease A, a truncated version of S-peptide (residues 1-15) and S-protein (residues 21-124), combine to give a catalytically active complex. We have substituted the wild-type residue at position 13, methionine (Met), with norleucine (Nle), where the only covalent change is the replacement of the sulfur atom with a methylene group. The thermodynamic parameters associated with the binding of this variant to S-protein, determined by titration calorimetry in the temperature range 10-40 degrees C, are reported and compared to values previously reported [Varadarajan, R., Connelly, P. R., Sturtevant, J. M., & Richards, F. M. (1992) Biochemistry 31, 1421-1426] for other position 13 analogs. The differences in the free energy and enthalpy of binding between the Met and Nle peptides are 0.6 and 7.9 kcal/mol at 25 degrees C, respectively. These differences are slightly larger than, but comparable to, the differences in the values for the Met/Ile and Met/Leu pairs. The structure of the mutant complex was determined to 1.85 A resolution and refined to an R-factor of 17.4%. The structures of mutant and wild-type complexes are practically identical although the Nle side chain has a significantly higher average B-factor than the corresponding Met side chain. In contrast, the B-factors of the atoms of the cage of residues surrounding position 13 are all somewhat lower in the Nle variant than the Met wild-type.(ABSTRACT TRUNCATED AT 250 WORDS)
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8031793}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8031793 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8031793}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ratnaparkhi, G.]] | | [[Category: Ratnaparkhi, G.]] |
| | [[Category: Varadarajan, R.]] | | [[Category: Varadarajan, R.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:08:22 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:04:26 2008'' |
Revision as of 17:04, 28 July 2008
Template:STRUCTURE 2rln
THERMODYNAMIC AND STRUCTURAL CONSEQUENCES OF CHANGING A SULPHUR ATOM TO A METHYLENE GROUP IN THE M13NLE MUTATION IN RIBONUCLEASE S
Template:ABSTRACT PUBMED 8031793
About this Structure
2RLN is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Thermodynamic and structural consequences of changing a sulfur atom to a methylene group in the M13Nle mutation in ribonuclease-S., Thomson J, Ratnaparkhi GS, Varadarajan R, Sturtevant JM, Richards FM, Biochemistry. 1994 Jul 19;33(28):8587-93. PMID:8031793
Page seeded by OCA on Mon Jul 28 20:04:26 2008
