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.


1wzb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wzb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1wzb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wzb| PDB=1wzb | SCENE= }}
{{STRUCTURE_1wzb| PDB=1wzb | SCENE= }}
-
'''Crystal structure of the collagen triple helix model [{HYP(R)-HYP(R)-GLY}10]3'''
+
===Crystal structure of the collagen triple helix model [{HYP(R)-HYP(R)-GLY}10]3===
-
==Overview==
+
<!--
-
X-ray analysis has been carried out on a crystal of the collagen model peptide (Hyp(R)-Hyp(R)-Gly)10 [where Hyp(R) is 4(R)-hydroxyproline] with 1.5 A resolution. The triple-helical structure of (Hyp(R)-Hyp(R)-Gly)10 has the same helical parameters and Rich and Crick II hydrogen bond patterns as those of other collagen model peptides. However, our full-length crystal structure revealed that almost all consecutive Hyp(R) residues take the up-up pucker in contrast to putative down-up puckering propensities of other collagen model peptides. The unique feature of thermodynamic parameters associated with the conformational transition of this peptide from triple helix to single coil is that both enthalpy and entropy changes of the transition are much smaller than those of other model peptides such as (Pro-Pro-Gly)10 and (Pro-Hyp(R)-Gly)10. To corroborate the precise structural information including main- and side-chain dihedral angles and intra- and interwater bridge networks, we estimated the degrees of hydration by comparing molecular volumes observed experimentally in solution to those calculated ones from the crystal structure. The results showed that the degree of hydration of (Hyp(R)-Hyp(R)-Gly)10 is comparable to that of (Pro-Hyp(R)-Gly)10 in the triple-helical state, but the former was more highly hydrated than (Pro-Hyp(R)-Gly)10 in the single-coil state. Because hydration reduces the enthalpy due to the formation of a hydrogen bond with a water molecule and diminishes the entropy due to the restriction of water molecules surrounding a peptide molecule, we concluded that the high thermal stability of (Hyp(R)-Hyp(R)-Gly)10 is able to be described by its high hydration in the single-coil state.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16313184}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16313184 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16313184}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Puckering]]
[[Category: Puckering]]
[[Category: Triple helix]]
[[Category: Triple helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:20:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:05:24 2008''

Revision as of 10:05, 27 July 2008

Image:1wzb.png

Template:STRUCTURE 1wzb

Crystal structure of the collagen triple helix model [{HYP(R)-HYP(R)-GLY}10]3

Template:ABSTRACT PUBMED 16313184

About this Structure

Full crystallographic information is available from OCA.

Reference

Effect of hydration on the stability of the collagen-like triple-helical structure of [4(R)-hydroxyprolyl-4(R)-hydroxyprolylglycine]10., Kawahara K, Nishi Y, Nakamura S, Uchiyama S, Nishiuchi Y, Nakazawa T, Ohkubo T, Kobayashi Y, Biochemistry. 2005 Dec 6;44(48):15812-22. PMID:16313184

Page seeded by OCA on Sun Jul 27 13:05:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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