منابع مشابه
Solvent accessible surface of globular proteins: how exposed and buried amino acid residues are divided
Introduction Globular protein structures are often divided into two regions, the surface, which is in contact with the surrounding molecules, and the interior, which is not accessible to the external molecules. Since most of the surrounding molecules, both in vitro and in vivo, are water molecules, it is clear that protein surface is essentially polar in order to make the protein molecule solub...
متن کاملPrediction of buried helices in multispan alpha helical membrane proteins.
Analysis of a database of structures of membrane proteins shows that membrane proteins composed of 10 or more transmembrane (TM) helices often contain buried helices that are inaccessible to phospholipids. We introduce a method for identifying TM helices that are least phospholipid accessible and for prediction of fully buried TM helices in membrane proteins from sequence information alone. Our...
متن کاملElectric field-induced polarization of charged cell surface proteins does not determine the direction of galvanotaxis.
Galvanotaxis, that is, migration induced by DC electric fields, is thought to play a significant role in development and wound healing, however, the mechanisms by which extrinsic electric fields orchestrate intrinsic motility responses are unknown. Using mammalian cell lines (3T3, HeLa, and CHO cells), we tested one prevailing hypothesis, namely, that electric fields polarize charged cell surfa...
متن کاملTolerance to the substitution of buried apolar residues by charged residues in the homologous protein structures.
Occurrence and accommodation of charged amino acid residues in proteins that are structurally equivalent to buried non-polar residues in homologues have been investigated. Using a dataset of 1,852 homologous pairs of crystal structures of proteins available at 2A or better resolution, 14,024 examples of apolar residues in the structurally conserved regions replaced by charged residues in homolo...
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ژورنال
عنوان ژورنال: Structure
سال: 2000
ISSN: 0969-2126
DOI: 10.1016/s0969-2126(00)00520-7