We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1ssz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ssz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ssz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ssz| PDB=1ssz | SCENE= }}
{{STRUCTURE_1ssz| PDB=1ssz | SCENE= }}
-
'''Conformational mapping of mini-b: an n-terminal/c-terminal construct of surfactant protein b using 13c-enhanced fourier transform infrared (FTIR) spectroscopy'''
+
===Conformational mapping of mini-b: an n-terminal/c-terminal construct of surfactant protein b using 13c-enhanced fourier transform infrared (FTIR) spectroscopy===
-
==Overview==
+
<!--
-
Surfactant protein B (SP-B) is essential for normal lung surfactant function. Theoretical models predict that the disulfide cross-linked, N- and C-terminal domains of SP-B fold as charged amphipathic helices, and suggest that these adjacent helices participate in critical surfactant activities. This hypothesis is tested using a disulfide-linked construct (Mini-B) based on the primary sequences of the N- and C-terminal domains. Consistent with theoretical predictions of the full-length protein, both isotope-enhanced Fourier transform infrared (FTIR) spectroscopy and molecular modeling confirm the presence of charged amphipathic alpha-helices in Mini-B. Similar to that observed with native SP-B, Mini-B in model surfactant lipid mixtures exhibits marked in vitro activity, with spread films showing near-zero minimum surface tensions during cycling using captive bubble surfactometry. In vivo, Mini-B shows oxygenation and dynamic compliance that compare favorably with that of full-length SP-B. Mini-B variants (i.e. reduced disulfides or cationic residues replaced by uncharged residues) or Mini-B fragments (i.e. unlinked N- and C-terminal domains) produced greatly attenuated in vivo and in vitro surfactant properties. Hence, the combination of structure and charge for the amphipathic alpha-helical N- and C-terminal domains are key to SP-B function.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16316452}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16316452 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16316452}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Lung surfactant protein]]
[[Category: Lung surfactant protein]]
[[Category: Saposin]]
[[Category: Saposin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:06:20 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:16:52 2008''

Revision as of 03:16, 29 July 2008

Image:1ssz.png

Template:STRUCTURE 1ssz

Conformational mapping of mini-b: an n-terminal/c-terminal construct of surfactant protein b using 13c-enhanced fourier transform infrared (FTIR) spectroscopy

Template:ABSTRACT PUBMED 16316452

About this Structure

1SSZ is a Single protein structure. Full crystallographic information is available from OCA.

Reference

The role of charged amphipathic helices in the structure and function of surfactant protein B., Waring AJ, Walther FJ, Gordon LM, Hernandez-Juviel JM, Hong T, Sherman MA, Alonso C, Alig T, Braun A, Bacon D, Zasadzinski JA, J Pept Res. 2005 Dec;66(6):364-74. PMID:16316452

Page seeded by OCA on Tue Jul 29 06:16:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ssz"
Personal tools