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| - | [[Image:1ytc.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ytc| PDB=1ytc | SCENE= }} | | {{STRUCTURE_1ytc| PDB=1ytc | SCENE= }} |
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| - | '''THERMODYNAMIC CYCLES AS PROBES OF STRUCTURE-FUNCTION RELATIONSHIPS IN UNFOLDED PROTEINS'''
| + | ===THERMODYNAMIC CYCLES AS PROBES OF STRUCTURE-FUNCTION RELATIONSHIPS IN UNFOLDED PROTEINS=== |
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| - | ==Overview==
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| - | The relationship between structure and stability has been investigated for the folded forms and the unfolded forms of iso-2 cytochrome c and a variant protein with a stability-enhancing mutation, N52I iso-2. Differential scanning calorimetry has been used to measure the reversible unfolding transitions for the proteins in both heme oxidation states. Reduction potentials have been measured as a function of temperature for the folded forms of the proteins. The combination of measurements of thermal stability and reduction potential gives three sides of a thermodynamic cycle and allows prediction of the reduction potential of the thermally unfolded state. The free energies of electron binding for the thermally unfolded proteins differ from those expected for a fully unfolded protein, suggesting that residual structure modulates the reduction potential. At temperatures near 50 degrees C the N52I mutation has a small but significant effect on oxidation state-sensitive structure in the thermally unfolded protein. Inspection of the high-resolution X-ray crystallographic structures of iso-2 and N52I iso-2 shows that the effects of the N52I mutation and oxidation state on native protein stability are correlated with changes in the mobility of specific polypeptide chain segments and with altered hydrogen bonding involving a conserved water molecule. However, there is no clear explanation of oxidation state or mutation-induced differences in stability of the proteins in terms of observed changes in structure and mobility of the folded forms of the proteins alone. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8639684}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8639684 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8639684}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Brayer, G D.]] | | [[Category: Brayer, G D.]] |
| | [[Category: Luo, Y.]] | | [[Category: Luo, Y.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:45:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:48:08 2008'' |
Revision as of 07:48, 28 July 2008
Template:STRUCTURE 1ytc
THERMODYNAMIC CYCLES AS PROBES OF STRUCTURE-FUNCTION RELATIONSHIPS IN UNFOLDED PROTEINS
Template:ABSTRACT PUBMED 8639684
About this Structure
1YTC is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Thermodynamic cycles as probes of structure in unfolded proteins., McGee WA, Rosell FI, Liggins JR, Rodriguez-Ghidarpour S, Luo Y, Chen J, Brayer GD, Mauk AG, Nall BT, Biochemistry. 1996 Feb 13;35(6):1995-2007. PMID:8639684
Page seeded by OCA on Mon Jul 28 10:48:08 2008
