1l05: Difference between revisions

Revision as of 14:39, 21 February 2008

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME

OverviewOverview

Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions.

About this StructureAbout this Structure

1L05 is a Single protein structure of sequence from Bacteriophage t4. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

ReferenceReference

Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme., Alber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW, Nature. 1987 Nov 5-11;330(6143):41-6. PMID:3118211

Page seeded by OCA on Thu Feb 21 13:39:49 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1l05.gif|left|200px]]<br /><applet load="1l05" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1l05.gif|left|200px]]<br /><applet load="1l05" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1l05, resolution 1.7&Aring;" />
 '''CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME'''<br />
 ==Overview==
-Measurements of changes in structure and stability caused by 13 different, substitutions for threonine 157 in phage T4 lysozyme show that the most, stable lysozyme variants contain hydrogen bonds analogous to those in the, wild-type enzyme and that structural adjustments allow the protein to be, surprisingly tolerant of amino-acid substitutions.
+Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions.
 ==About this Structure==
-L05 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L05 OCA].
+L05 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L05 OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Alber, T.]]
 [[Category: Dao-Pin, S.]]
-[[Category: Matthews, B.W.]]
+[[Category: Matthews, B W.]]
 [[Category: hydrolase (o-glycosyl)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:06:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:49 2008''