scholarly journals Improvement of student understanding of how kinetic data facilitates the determination of amino acid catalytic function through an alkaline phosphatase structure/mechanism bioinformatics exercise

2008 ◽  
Vol 36 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Sandra K. Grunwald ◽  
Katherine J. Krueger
Keyword(s):  
Alkaline Phosphatase ◽  
Amino Acid ◽  
Kinetic Data ◽  
Student Understanding ◽  
Catalytic Function

Simultaneous Determinations of Liver- and Bone-Type Alkaline Phosphatase by Curve-Fitting of Inhibition Kinetic Data. II. Development and Evaluation of a Fluorescence-Based Method

1992 ◽  
Vol 38 (2) ◽  
pp. 247-255 ◽  
Author(s):  
Carol P Fitzpatrick ◽  
Harry L Pardue
Keyword(s):  
Alkaline Phosphatase ◽  
Kinetic Data ◽  
Kinetic Method ◽  
Linear Least Squares ◽  
First Order ◽  
Least Squares Fit ◽  
Inhibition Kinetic ◽  
Substrate Concentrations ◽  
Measurement Period

Abstract We describe a kinetic method for the determination of alkaline phosphatase (ALP) isoenzymes, based on fluorescence detection of 4-methylumbelliferone. Several different buffer-inhibitor combinations and substrate concentrations were evaluated. Best results were obtained for inhibition with 2.9 mol/L urea in amino-2-methyl-1-propanol buffer. With this combination, normal concentrations of bone- and liver-type ALP could be determined from kinetic data during an 8-min measurement period. We computed initial velocities from parameters for first-order fits during 1.2 half-lives of the response for liver-type ALP. A linear least-squares fit of initial velocities (y) determined in this way vs results obtained with a comparison procedure (x) gave good correlations. We also estimated total signal changes, delta S, from first-order fits during four half-lives. Isoenzyme content correlated well with parameters computed from the first-order fits. Values for standard errors of the estimates represent 5% and 3% of median responses for activities and isoenzyme content, respectively. When compared with an absorbance-based method described previously, this method had threefold shorter measurement times, but imprecisions were 1.6- to 1.8-fold larger.

Polypeptides Folding: Rules for the Calculation of the Backbone Dihedral Angles φ starting from the Amino Acid Sequence

2020 ◽  
Author(s):  
Michele Larocca
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Theoretical Approach ◽  
Polypeptide Chain ◽  
Hydrophobic Effect ◽  
Side Chain ◽  
Dihedral Angles ◽  
Mechanical Forces ◽  
Specific Chemical

<p>Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.</p>

scholarly journals A Method for the Determination of Some Amino Acid Decarboxylases

1960 ◽  
Vol 235 (1) ◽  
pp. 124-127
Author(s):  
Virginia E. Davis ◽  
J. Awapara
Keyword(s):  
Amino Acid
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