This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1zwc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zwc.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zwc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zwc| PDB=1zwc | SCENE= }}
{{STRUCTURE_1zwc| PDB=1zwc | SCENE= }}
-
'''STRUCTURE OF BOVINE PARATHYROID HORMONE FRAGMENT 1-37, NMR, 10 STRUCTURES'''
+
===STRUCTURE OF BOVINE PARATHYROID HORMONE FRAGMENT 1-37, NMR, 10 STRUCTURES===
-
==Overview==
+
<!--
-
Parathyroid hormone (PTH) is involved in regulation of the calcium level in blood and has an influence on bone metabolism, thus playing a role in osteoporosis therapy. In this study, the structures of the human PTH fragments (1-34) and (1-39) as well as bovine PTH(1-37) in aqueous buffer solution under near physiological conditions were determined using two-dimensional nuclear magnetic resonance spectroscopy. The overall structure of the first 34 amino acids of these three peptides is virtually identical, exhibiting a short NH(2)-terminal and a longer COOH-terminal helix as well as a defined loop region from His14 to Ser17, stabilized by hydrophobic interactions. bPTH(1-37), which has a higher biological activity, shows a better-defined NH(2)-terminal part. In contrast to NH(2)-terminal truncations, which cause destabilization of helical structure, neither COOH-terminal truncation nor elongation significantly influences the secondary structure. Furthermore, we investigated the structure of hPTH(1-34) in 20% trifluoroethanol solution. In addition to its helix-stabilizing effect, trifluorethanol causes the loss of tertiary hydrophobic interactions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10623601}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10623601 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10623601}}
==About this Structure==
==About this Structure==
-
1ZWC is a [[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=1ZWC OCA].
+
1ZWC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZWC OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: Hormone]]
[[Category: Hormone]]
[[Category: Signal]]
[[Category: Signal]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:09:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:18:30 2008''

Revision as of 11:18, 29 July 2008

Image:1zwc.png

Template:STRUCTURE 1zwc

STRUCTURE OF BOVINE PARATHYROID HORMONE FRAGMENT 1-37, NMR, 10 STRUCTURES

Template:ABSTRACT PUBMED 10623601

About this Structure

1ZWC is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

Reference

Solution structures of human parathyroid hormone fragments hPTH(1-34) and hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37)., Marx UC, Adermann K, Bayer P, Forssmann WG, Rosch P, Biochem Biophys Res Commun. 2000 Jan 7;267(1):213-20. PMID:10623601

Page seeded by OCA on Tue Jul 29 14:18:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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