1xpt: Difference between revisions

Revision as of 06:45, 29 July 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:1xpt.png

Template:STRUCTURE 1xpt

BOVINE RIBONUCLEASE A (PHOSPHATE-FREE)BOVINE RIBONUCLEASE A (PHOSPHATE-FREE)

Template:ABSTRACT PUBMED 10089510

About this StructureAbout this Structure

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

ReferenceReference

Plasticity, hydration and accessibility in ribonuclease A. The structure of a new crystal form and its low-humidity variant., Sadasivan C, Nagendra HG, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1343-52. PMID:10089510

Page seeded by OCA on Tue Jul 29 06:45:26 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1xpt.jpg|left|200px]]
+{{Seed}}
+[[Image:1xpt.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1xpt|  PDB=1xpt  |  SCENE=  }}
-'''BOVINE RIBONUCLEASE A (PHOSPHATE-FREE)'''
+===BOVINE RIBONUCLEASE A (PHOSPHATE-FREE)===
-==Overview==
+<!--
-The structures of a new crystal form of ribonuclease A and its low-humidity variant, each containing two crystallographically independent molecules, have been determined and refined. A detailed comparison of these structures with those of the other known crystal forms of the enzyme, which have different packing arrangements and solvent composition, leads to a meaningful delineation of the rigid and flexible regions of the protein molecule and the nature of its plasticity. Many of the water molecules which are common to all the structures are involved in bridging different regions of the protein molecule, thus emphasizing the role of water in stabilizing the tertiary structure. The analysis of the structures shows that for a given N or O atom, the level of hydration increases with accessible surface area, but levels off at an area of about 10 A2. Generally, the hydration level tends to drop when the area increases beyond about 20 A2. This drop correlates with an increase in the displacement parameter. The analysis also suggests that the van der Waals radii and probe radius normally used in accessible surface area calculations are not appropriate for dealing with all situations.
+The line below this paragraph, {{ABSTRACT_PUBMED_10089510}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10089510 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10089510}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Sadasivan, C.]]
 [[Category: Vijayan, M.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 15:20:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:45:26 2008''