Hydrophobic, Hydrophilic, and Charged Amino Acid Networks within Protein
نویسندگان
چکیده
منابع مشابه
Hydrophobic, hydrophilic, and charged amino acid networks within protein.
The native three-dimensional structure of a single protein is determined by the physicochemical nature of its constituent amino acids. The 20 different types of amino acids, depending on their physicochemical properties, can be grouped into three major classes: hydrophobic, hydrophilic, and charged. The anatomy of the weighted and unweighted networks of hydrophobic, hydrophilic, and charged res...
متن کاملNPPD: A Protein-Protein Docking Scoring Function Based on Dyadic Differences in Networks of Hydrophobic and Hydrophilic Amino Acid Residues
Protein-protein docking (PPD) predictions usually rely on the use of a scoring function to rank docking models generated by exhaustive sampling. To rank good models higher than bad ones, a large number of scoring functions have been developed and evaluated, but the methods used for the computation of PPD predictions remain largely unsatisfactory. Here, we report a network-based PPD scoring func...
متن کاملProtein contact networks at different length scales and role of hydrophobic, hydrophilic and charged residues in protein's structural organisation
acids in primary chain, the contact networks are constructed based on the 3D spatial distances of amino acids. We have further divided these networks into sub-networks of hydrophobic, hydrophilic and charged residues. Our analysis reveals that a significantly higher percentage of assortative sub-clusters of long-range hydrophobic networks helps a protein in communicating the necessary informati...
متن کاملA Soluble, Folded Protein without Charged Amino Acid Residues.
Charges are considered an integral part of protein structure and function, enhancing solubility and providing specificity in molecular interactions. We wished to investigate whether charged amino acids are indeed required for protein biogenesis and whether a protein completely free of titratable side chains can maintain solubility, stability, and function. As a model, we used a cellulose-bindin...
متن کاملSurface hydrophobic and hydrophilic protein alterations in Candida albicans.
Cell surface hydrophobicity influences pathogenesis of Candida albicans. Previous studies suggested that stationary-phase hydrophilic and hydrophobic cells, obtained by growth at 37 and 23 degrees C, respectively, may have similar hydrophobic proteins. However, whether hydrophilic and hydrophobic surface proteins differ during the growth cycle at 37 degrees C is unknown. Freeze-fracture analysi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2007
ISSN: 0006-3495
DOI: 10.1529/biophysj.106.098004