1c98: Difference between revisions

Revision as of 20:23, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1c98.png

Template:STRUCTURE 1c98

SOLUTION STRUCTURE OF NEUROMEDIN BSOLUTION STRUCTURE OF NEUROMEDIN B

Template:ABSTRACT PUBMED 10544247

About this StructureAbout this Structure

1C98 is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

Solution structure of neuromedin B by (1)H nuclear magnetic resonance spectroscopy., Lee S, Kim Y, FEBS Lett. 1999 Oct 29;460(2):263-9. PMID:10544247

Page seeded by OCA on Mon Jun 30 20:23:46 2008

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OCA

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-[[Image:1c98.gif|left|200px]]
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 {{STRUCTURE_1c98|  PDB=1c98  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF NEUROMEDIN B'''
+===SOLUTION STRUCTURE OF NEUROMEDIN B===
-==Overview==
+<!--
-The solution structure of neuromedin B (NMB) was investigated using two-dimensional nuclear magnetic resonance (NMR) spectroscopy in membrane-mimicking environments. NMB adopts a relaxed helical conformation from Trp(4) to Met(10) in 50% aqueous 2,2, 2-trifluoroethanol (TFE) solution and in 150 mM SDS micelles. Sidechain atoms of the three residues, Trp(4), His(8) and Phe(9) orient toward the same direction and these residues might play a key role on interacting with hydrophobic acyl chains of the phospholipids in the membrane. NOESY experiments performed on NMB in non-deuterated SDS micelle show that aromatic ring protons of Trp(4) and Phe(9) residues are in close contact with methylene protons of SDS micelles. In addition, proton longitudinal relaxation data proved that the interactions between NMB with SDS micelle are characterized as extrinsic interaction. Trp(4) and Phe(9) seem to be important in interaction with receptor and this agrees with the previous studies of structure-activity relationship (Howell, D.C. et al. (1996) Int. J. Pept. Protein Res. 48, 522-531). These conformational features might be helpful in understanding the molecular mechanism of the function of NMB and developing the efficient drugs.
+The line below this paragraph, {{ABSTRACT_PUBMED_10544247}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10544247 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10544247}}
 ==About this Structure==
-C98 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C98 OCA].
+C98 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C98 OCA].
 ==Reference==
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 [[Category: Nmr]]
 [[Category: Peptide]]
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