1l05: Difference between revisions

Revision as of 23:23, 2 May 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 Enterobacteria phage t4. 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 Fri May 2 23:23:27 2008

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OCA

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 [[Image:1l05.gif|left|200px]]
- {{Structure
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-}}
 '''CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME'''
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 [[Category: Dao-Pin, S.]]
 [[Category: Matthews, B W.]]
-[[Category: hydrolase (o-glycosyl)]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:23:27 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:09 2008''