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| | {{STRUCTURE_1his| PDB=1his | SCENE= }} | | {{STRUCTURE_1his| PDB=1his | SCENE= }} |
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| - | '''STRUCTURE AND DYNAMICS OF DES-PENTAPEPTIDE-INSULIN IN SOLUTION: THE MOLTEN-GLOBULE HYPOTHESIS'''
| + | ===STRUCTURE AND DYNAMICS OF DES-PENTAPEPTIDE-INSULIN IN SOLUTION: THE MOLTEN-GLOBULE HYPOTHESIS=== |
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| - | ==Overview==
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| - | Structures of insulin in different crystal forms exhibit significant local and nonlocal differences, including correlated displacement of elements of secondary structure. Here we describe the solution structure and dynamics of a monomeric insulin analogue, des-pentapeptide-(B26-B30)-insulin (DPI), as determined by two-dimensional NMR spectroscopy and distance geometry/restrained molecular dynamics (DG/RMD). Although the solution structure of DPI exhibits a general similarity to its crystal structure, individual DG/RMD structures in the NMR ensemble differ by rigid-body displacements of alpha-helices that span the range of different crystal forms. These results suggest that DPI exists as a partially folded state formed by coalescence of distinct alpha-helix-associated microdomains. The physical reality of this model is investigated by comparison of the observed two-dimensional nuclear Overhauser enhancement (NOE) spectroscopy (NOESY) spectrum with that predicted from crystal and DG/RMD structures. The observed NOESY spectrum contains fewer tertiary contacts than predicted by any single simulation, but it matches their shared features; such "ensemble correspondence" is likely to reflect the effect of protein dynamics on observed NOE intensities. We propose (i) that the folded state of DPI is analogous to that of a compact protein-folding intermediate rather than a conventional native state and (ii) that the molten state is the biologically active species. This proposal (the molten-globule hypothesis) leads to testable thermodynamic predictions and has general implications for protein design.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_1549601}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 1549601 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_1549601}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1HIS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIS OCA]. | + | 1HIS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HIS OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Weiss, M A.]] | | [[Category: Weiss, M A.]] |
| | [[Category: Hormone]] | | [[Category: Hormone]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:53:07 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:14:26 2008'' |
Revision as of 05:14, 1 July 2008
Template:STRUCTURE 1his
STRUCTURE AND DYNAMICS OF DES-PENTAPEPTIDE-INSULIN IN SOLUTION: THE MOLTEN-GLOBULE HYPOTHESIS
Template:ABSTRACT PUBMED 1549601
About this Structure
1HIS is a Protein complex structure of sequences from Homo sapiens. Full experimental information is available from OCA.
Reference
Structure and dynamics of des-pentapeptide-insulin in solution: the molten-globule hypothesis., Hua QX, Kochoyan M, Weiss MA, Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2379-83. PMID:1549601
Page seeded by OCA on Tue Jul 1 08:14:26 2008
