Joint neighbors approximation of macromolecular solvent accessible surface area

نویسندگان

  • Georgy Rychkov
  • Michael Petukhov
چکیده

A new method for approximate analytical calculations of solvent accessible surface area (SASA) for arbitrary molecules and their gradients with respect to their atomic coordinates was developed. This method is based on the recursive procedure of pairwise joining of neighboring atoms. Unlike other available methods of approximate SASA calculations, the method has no empirical parameters, and therefore can be used with comparable accuracy in calculations of SASA in folded and unfolded conformations of macromolecules of any chemical nature. As shown by tests with globular proteins in folded conformations, average errors in absolute atomic surface area is around 1 A2, while for unfolded protein conformations it varies from 1.65 to 1.87 A2. Computational times of the method are comparable with those by GETAREA, one of the fastest exact analytical methods available today.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Molecular multiresolution surfaces

The surface of a molecule determines much of its chemical and physical property, and is of great interest and importance. In this Letter, we introduce the concept of molecular multiresolution surfaces as a new paradigm of multiscale biological modeling. Molecular multiresolution surfaces contain not only a family of molecular surfaces, corresponding to different probe radii, but also the solven...

متن کامل

Introducing critical residues in the human prion protein and its Asp 178 Asn mutant by molecular dynamics simulation

The molecular dynamics (MD) simulation method is used to assess structural details for humanprion protein (hereafter PrPN) and its Asp178 Asn mutant (hereafter PrPm) which causes fatalfamilial insomnia disease. The results reveal that the flexibility and instability increase in PrPmcould be related to specific amino acids exposed to the solvent. Solvation free energy of PrPm is 20kjmot1nni2 mor...

متن کامل

Development of Residue Look-Up Tables and Graphical Representation of Solvent Accessibility in Proteins

We previously developed the first method to predict real valued accessible surface area in proteins, which was shown to contain more information than 100% correct predictions in a binary space of exposure states. Neural networks used for solvent accessibility predictions, however work as good predictors with invisible modeling of knowledge they learn. In view of this a direct statistical analys...

متن کامل

A Simulated Annealing Algorithm for Geometrical Assessment of Macromolecular Hydrophobic Interaction

Macromolecular interaction is critical to many biological and biochemical processes and phenomena in living systems. Its assessment would lead to a deeper understanding of many relevant phenomena at the molecular level such as molecular and cellular recognition, signal transmission, and many other processes in life systems, as well as in drug and protein engineering. It is widely recognized tha...

متن کامل

Parameter optimized surfaces (POPS): analysis of key interactions and conformational changes in the ribosome

We present a new method for the calculation of solvent accessible surface areas at the atomic and residue levels, which we call parameter optimized surfaces (POPS-A and POPS-R ). Atomic and residue areas (the latter simulated with a single sphere centered at the C(alpha)s atom for amino acids and at the P atom for nucleotides) have been optimized versus accurate all-atoms methods. We concentrat...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Journal of computational chemistry

دوره 28 12  شماره 

صفحات  -

تاریخ انتشار 2007