Direct Determination of Site-Specific Noncovalent Interaction Strengths of Proteins from NMR-Derived Fast Side Chain Motional Parameters

2017 ◽  
Vol 121 (20) ◽  
pp. 5174-5186 ◽  
Author(s):  
Rajitha Rajeshwar T ◽  
Marimuthu Krishnan
Keyword(s):  
Direct Determination ◽  
Noncovalent Interaction ◽  
Side Chain ◽  
Site Specific

The Direct Determination of I131 in Heterogeneous Fecal Specimens

1961 ◽  
Vol 41 (4) ◽  
pp. 380-384 ◽  
Author(s):  
Arthur F. Dratz ◽  
James C. Coberly
Keyword(s):  
Direct Determination

A New Method for Direct Determination of the Recoilless Fraction with Application to Magnetic Nanoparticles

2002 ◽  
Vol 721 ◽  
Author(s):  
Monica Sorescu
Keyword(s):  
Room Temperature ◽  
Average Particle Size ◽  
Direct Determination ◽  
Average Particle ◽  
Lattice Method ◽  
Recoilless Fraction ◽  
Single Room ◽  
Magnetite Particles ◽  
Physical Mixtures

AbstractWe propose a two-lattice method for direct determination of the recoilless fraction using a single room-temperature transmission Mössbauer measurement. The method is first demonstrated for the case of iron and metallic glass two-foil system and is next generalized for the case of physical mixtures of two powders. We further apply this method to determine the recoilless fraction of hematite and magnetite particles. Finally, we provide direct measurement of the recoilless fraction in nanohematite and nanomagnetite with an average particle size of 19 nm.

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>

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