1kf4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1kf4.jpg|left|200px]]
{{Seed}}
[[Image:1kf4.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kf4|  PDB=1kf4  |  SCENE=  }}  
{{STRUCTURE_1kf4|  PDB=1kf4  |  SCENE=  }}  


'''Atomic Resolution Structure of RNase A at pH 6.3'''
===Atomic Resolution Structure of RNase A at pH 6.3===




==Overview==
<!--
The diffraction pattern of protein crystals extending to atomic resolution guarantees a very accurate picture of the molecular structure and enables the study of subtle phenomena related to protein functionality. Six structures of bovine pancreatic ribonuclease at the pH* values 5.2, 5.9, 6.3, 7.1, 8.0 and 8.8 and at resolution limits in the range 1.05-1.15A have been refined. An overall description of the six structures and several aspects, mainly regarding pH-triggered conformational changes, are described here. Since subtle variations were expected, a thorough validation assessment of the six refined models was first carried out. Some stereochemical parameters, such as the N[bond]C(alpha)[bond]C angle and the pyramidalization at the carbonyl C atoms, indicate that the standard target values and their weights typically used in refinement may need revision. A detailed comparison of the six structures has provided experimental evidence on the role of Lys41 in catalysis. Furthermore, insights are given into the structural effects related to the pH-dependent binding of a sulfate anion, which mimics the phosphate group of RNA, in the active site. Finally, the results support a number of thermodynamic and kinetic experimental data concerning the role of the disulfide bridge between Cys65 and Cys72 in the folding of RNase A.
The line below this paragraph, {{ABSTRACT_PUBMED_11856829}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11856829 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11856829}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Soaking]]
[[Category: Soaking]]
[[Category: Titration]]
[[Category: Titration]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:40:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:14:56 2008''

Revision as of 07:15, 2 July 2008

File:1kf4.png

Template:STRUCTURE 1kf4

Atomic Resolution Structure of RNase A at pH 6.3

Template:ABSTRACT PUBMED 11856829

About this Structure

1KF4 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Atomic resolution structures of ribonuclease A at six pH values., Berisio R, Sica F, Lamzin VS, Wilson KS, Zagari A, Mazzarella L, Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):441-50. Epub 2002, Feb 21. PMID:11856829

Page seeded by OCA on Wed Jul 2 10:14:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1kf4&oldid=620545"