How Long to Read Solute-Solvent Interactions in Folded and Unfolded Proteins

How Long Does it Take to Read Solute-Solvent Interactions in Folded and Unfolded Proteins?

It takes the average reader 7 hours and 35 minutes to read Solute-Solvent Interactions in Folded and Unfolded Proteins by Soyoung Lee

Assuming a reading speed of 250 words per minute. Learn more

Description

This thesis is devoted to understanding solute-solvent interactions in folded and unfolded proteins. To this end, we have studied partial molar volume, V°, and adiabatic compressibility, K°S, of 20 amino acid side chains using low weight molecular model compounds, N-acetyl amino acid amide and its derivatives, between 18°C and 55°C. We used our data to develop an additive scheme for calculating the partial specific volume and adiabatic compressibility of fully extended polypeptide chains as a function of pH and temperature. We compared our calculated volumetric characteristics of the fully extended conformations of apocytochrome c and apomyoglobin with the experimental values measured in neutral pH (for apocytochrome c) or acidic pH (for apomyoglobin). The comparison between the calculated and experimental volumetric characteristics suggested that neither apocytochrome c nor apomyoglobin are fully unfolded and retain solvent-inaccessible amino acid residues. To study cosolvent-solute interactions, we determined V° and K° S of amino acid side chains and glycyl units as a function of urea concentration. We analyzed these data within the framework of a statistical thermodynamic formalism to determine the association constants, k, for the reaction in which urea binds to each of the amino acid side chains and the glycyl unit replacing two water molecules in solvation shell. Our determined k range from 0.04 to 0.39 M with the average of 0.16 +/- 0.09 M. There was no apparent correlation between the values of k and the ratio of polar to nonpolar solvent accessible surface areas. This study supports a direct interaction model in which urea denatures a protein by concerted action via favorable interactions with a wide range of protein groups. In addition, we have presented buffer ionization effect on the volume of protein denaturation could be significant with the potential to affect not only its magnitude but also its sign using a pressure perturbation calorimetric technique. Our results identified buffer ionization as an important determinant of protein transition volume that needs to be carefully taken into account. Results described in this work provide fundamental understanding of solute-solvent interaction in both folded and unfolded proteins.

How long is Solute-Solvent Interactions in Folded and Unfolded Proteins?

Solute-Solvent Interactions in Folded and Unfolded Proteins by Soyoung Lee is 452 pages long, and a total of 113,904 words.

This makes it 153% the length of the average book. It also has 139% more words than the average book.

How Long Does it Take to Read Solute-Solvent Interactions in Folded and Unfolded Proteins Aloud?

The average oral reading speed is 183 words per minute. This means it takes 10 hours and 22 minutes to read Solute-Solvent Interactions in Folded and Unfolded Proteins aloud.

What Reading Level is Solute-Solvent Interactions in Folded and Unfolded Proteins?

Solute-Solvent Interactions in Folded and Unfolded Proteins is suitable for students ages 12 and up.

Note that there may be other factors that effect this rating besides length that are not factored in on this page. This may include things like complex language or sensitive topics not suitable for students of certain ages.

When deciding what to show young students always use your best judgement and consult a professional.

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