Abstract
This article reviews and discusses the relationship between surface hydrophobicity and other surface properties of proteins and the possibility of using surface hydrophobicity as a key indicator to predict and evaluate the changes in the surface properties of a protein. Hydrophobicity is the main driving force of protein folding; it affects the structure and functions. Surface hydrophobicity and other surface properties of proteins are controlled by their spatial structures. Due to the hydrophobic interactions, most proteins fold into their globular structures, and they lack sufficient hydrophobic residues on the molecular surface; thus, they do not exhibit excellent surface properties. Surface hydrophobicity is closely related to the changes in the surface property of proteins because it directly reflects the actual distribution of the hydrophobic residues on the surface of a protein. The molecular structure of a protein can be changed or modified to remove the constraints of spatial structures and expose more hydrophobic residues on the molecular surface, which may improve the surface properties of proteins. Therefore, the changes in the surface hydrophobicity caused by changes in the molecular structure can be an ideal key indicator to predict and evaluate the changes in the surface properties of a protein.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
