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.


1ssc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ssc.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ssc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ssc| PDB=1ssc | SCENE= }}
{{STRUCTURE_1ssc| PDB=1ssc | SCENE= }}
-
'''THE 1.6 ANGSTROMS STRUCTURE OF A SEMISYNTHETIC RIBONUCLEASE CRYSTALLIZED FROM AQUEOUS ETHANOL. COMPARISON WITH CRYSTALS FROM SALT SOLUTIONS AND WITH RNASE A FROM AQUEOUS ALCOHOL SOLUTIONS'''
+
===THE 1.6 ANGSTROMS STRUCTURE OF A SEMISYNTHETIC RIBONUCLEASE CRYSTALLIZED FROM AQUEOUS ETHANOL. COMPARISON WITH CRYSTALS FROM SALT SOLUTIONS AND WITH RNASE A FROM AQUEOUS ALCOHOL SOLUTIONS===
-
==Overview==
+
<!--
-
The non-covalent combination of residues 1-118 of RNase A with a synthetic 14-residue peptide containing residues 111-124 of the molecule forms a highly active semisynthetic enzyme, RNase 1-118:111-124. With this enzyme, the roles played by the six C-terminal residues in generating the catalytic efficiency and substrate specificity of RNase can be studied using chemically synthesized analogs. The structure of RNase 1-118:111-124 from 43% aqueous ethanol has been determined using molecular-replacement methods and refined to a crystallographic R-factor of 0.166 for all observed reflections in the range 7.0-1.6 A (Protein Data Bank file ISSC). The structure is compared with the 2.0 A structure of RNase A from 43% aqueous 2-methyl-2-propanol and with the 1.8 A structure of the semisynthetic enzyme obtained from crystals grown in concentrated salt solution. The structure of RNase 1-118:111-124 from aqueous ethanol is virtually identical to that of RNase A from aqueous 2-methyl-2-propanol. Half of the crystallographically bound water molecules are not coincident, however. The structure is somewhat less similar to that of RNase 1-118:111-124 from salt solutions, with a major difference being the positioning of active-site residue His119.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15299768}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15299768 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15299768}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Rodier, F.]]
[[Category: Rodier, F.]]
[[Category: Endonuclease]]
[[Category: Endonuclease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:05:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:43:34 2008''

Revision as of 06:43, 28 July 2008

Template:STRUCTURE 1ssc

THE 1.6 ANGSTROMS STRUCTURE OF A SEMISYNTHETIC RIBONUCLEASE CRYSTALLIZED FROM AQUEOUS ETHANOL. COMPARISON WITH CRYSTALS FROM SALT SOLUTIONS AND WITH RNASE A FROM AQUEOUS ALCOHOL SOLUTIONS

Template:ABSTRACT PUBMED 15299768

About this Structure

1SSC is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

Reference

1.6 A structure of semisynthetic ribonuclease crystallized from aqueous ethanol. Comparison with crystals from salt solutions and with ribonuclease A from aqueous alcohol solutions., de Mel SJ, Doscher MS, Martin PD, Rodier F, Edwards BF, Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):1003-12. PMID:15299768

Page seeded by OCA on Mon Jul 28 09:43:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools