1bba
From Proteopedia
(New page: 200px<br /><applet load="1bba" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bba" /> '''SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS AND SOL...) |
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'''SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS AND SOLUTION STRUCTURE OF BOVINE PANCREATIC POLYPEPTIDE'''<br /> | '''SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS AND SOLUTION STRUCTURE OF BOVINE PANCREATIC POLYPEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sequence-specific 1H NMR assignments for the 36 residue bovine pancreatic | + | Sequence-specific 1H NMR assignments for the 36 residue bovine pancreatic polypeptide (bPP) have been completed. The secondary and tertiary structure of bPP in solution has been determined from experimental NMR data. It is shown that bPP has a very well-defined C-terminal alpha-helix involving residues 15-32. Although regular secondary structure cannot be clearly defined in the N-terminal region, residues 4-8 maintain a rather ordered conformation in solution. This is attributed primarily to the hydrophobic interactions between this region and the C-terminal helix. The two segments of the structure are joined by a turn which is poorly defined. The four end residues both at the N-terminus and the C-terminus are highly disordered in solution. The overall fold of the bPP molecule is very closely similar to that found in the crystal structure of avian pancreatic polypeptide (aPP). The RMS deviation for backbone atoms of residues 4-8 and 15-32 between the bPP mean structure and the aPP crystal structure is 0.65 A, although there is only 39% identity of the residues. Furthermore, the average conformations of some (mostly from the alpha-helix) side chains of bPP in solution are closely similar to those of aPP in the crystal structure. A large number of side chains of bPP, however, show significant conformational averaging in solution. |
==About this Structure== | ==About this Structure== | ||
| - | 1BBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 1BBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BBA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dobson, C | + | [[Category: Dobson, C M.]] |
[[Category: Li, X.]] | [[Category: Li, X.]] | ||
| - | [[Category: Schwartz, T | + | [[Category: Schwartz, T W.]] |
| - | [[Category: Sutcliffe, M | + | [[Category: Sutcliffe, M J.]] |
[[Category: pancreatic hormone]] | [[Category: pancreatic hormone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:34 2008'' |
Revision as of 09:53, 21 February 2008
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SEQUENCE-SPECIFIC 1H NMR ASSIGNMENTS AND SOLUTION STRUCTURE OF BOVINE PANCREATIC POLYPEPTIDE
Overview
Sequence-specific 1H NMR assignments for the 36 residue bovine pancreatic polypeptide (bPP) have been completed. The secondary and tertiary structure of bPP in solution has been determined from experimental NMR data. It is shown that bPP has a very well-defined C-terminal alpha-helix involving residues 15-32. Although regular secondary structure cannot be clearly defined in the N-terminal region, residues 4-8 maintain a rather ordered conformation in solution. This is attributed primarily to the hydrophobic interactions between this region and the C-terminal helix. The two segments of the structure are joined by a turn which is poorly defined. The four end residues both at the N-terminus and the C-terminus are highly disordered in solution. The overall fold of the bPP molecule is very closely similar to that found in the crystal structure of avian pancreatic polypeptide (aPP). The RMS deviation for backbone atoms of residues 4-8 and 15-32 between the bPP mean structure and the aPP crystal structure is 0.65 A, although there is only 39% identity of the residues. Furthermore, the average conformations of some (mostly from the alpha-helix) side chains of bPP in solution are closely similar to those of aPP in the crystal structure. A large number of side chains of bPP, however, show significant conformational averaging in solution.
About this Structure
1BBA is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Sequence-specific 1H NMR assignments and solution structure of bovine pancreatic polypeptide., Li XA, Sutcliffe MJ, Schwartz TW, Dobson CM, Biochemistry. 1992 Feb 4;31(4):1245-53. PMID:1734969
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