scholarly journals FREQUENCY AND MARKOV CHAIN ANALYSIS OF THE AMINO-ACID SEQUENCE OF HUMAN ALCOHOL DEHYDROGENASE alpha-CHAIN

2000 ◽  
Vol 35 (3) ◽  
pp. 302-306 ◽  
Author(s):  
G. WU
2000 ◽  
Vol 19 (9) ◽  
pp. 535-539 ◽  
Author(s):  
G Wu

The amino acid sequence of mouse p53 was measured according to two-and three-amino-acid sequences. The measured frequency and probability were compared with predicted frequency and probability. Of 389 two-amino-acidsequencesinmousep53,85 (21.851%) and27 (6.941%) sequences can be explained by the predicted frequency and probability accordingto a purely random mechanism. Of 188 non-appearing two-amino-acid sequences in mouse p53, 86 (45.745%) and 32 (17.021%) can be explained by the predicted frequency and probability according to a purely random mechanism; no more than two-amino-acid sequences inmousep53 canbe explained by a purelyrandom mechanism.


1999 ◽  
Vol 31 (3) ◽  
pp. 611-622 ◽  
Author(s):  
Rhonda Skaggs ◽  
Soumen Ghosh

AbstractMarkov chain analysis (one-step and long-run) is applied to the National Resources Inventory (NRI) database to evaluate changes in wind-based soil erosion rates over time. The research compares changes in soil erosion rates between NRI sample sites with and without applied conservation practices for a random sample of Great Plains counties. No significant differences between sites are found for half of the counties evaluated. The effectiveness and efficiency of conservation policies are thus questioned in light of these research results.


2001 ◽  
Vol 183 (6) ◽  
pp. 1954-1960 ◽  
Author(s):  
Grit Zarnt ◽  
Thomas Schräder ◽  
Jan R. Andreesen

ABSTRACT The quinohemoprotein tetrahydrofurfuryl alcohol dehydrogenase (THFA-DH) from Ralstonia eutropha strain Bo was investigated for its catalytic properties. The apparentk cat/Km andK i values for several substrates were determined using ferricyanide as an artificial electron acceptor. The highest catalytic efficiency was obtained with n-pentanol exhibiting a k cat/Km value of 788 × 104 M−1 s−1. The enzyme showed substrate inhibition kinetics for most of the alcohols and aldehydes investigated. A stereoselective oxidation of chiral alcohols with a varying enantiomeric preference was observed. Initial rate studies using ethanol and acetaldehyde as substrates revealed that a ping-pong mechanism can be assumed for in vitro catalysis of THFA-DH. The gene encoding THFA-DH from R. eutropha strain Bo (tfaA) has been cloned and sequenced. The derived amino acid sequence showed an identity of up to 67% to the sequence of various quinoprotein and quinohemoprotein dehydrogenases. A comparison of the deduced sequence with the N-terminal amino acid sequence previously determined by Edman degradation analysis suggested the presence of a signal sequence of 27 residues. The primary structure of TfaA indicated that the protein has a tertiary structure quite similar to those of other quinoprotein dehydrogenases.


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