Distance-based NMR structure determination and refinement
نویسندگان
چکیده
The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleed-through, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion.
منابع مشابه
Distance-based protein structure modeling
Protein structure modeling can be studied based on the knowledge of interactions or distances between pairs of atoms, which is so-called distance-based protein structure modeling and this field includes problems of structure determination and refinement as well as analysis of protein dynamics. The distances for certain pairs of atoms in a protein can often be obtained based on our knowledge on ...
متن کاملTowards Automating Protein Structure Determination from NMR Data
Nuclear magnetic resonance (NMR) spectroscopy technique is becoming exceedingly significant due to its capability of studying protein structures in solution. However, NMR protein structure determination has remained a laborious and costly process until now, even with the help of currently available computer programs. After the NMR spectra are collected, the main road blocks to the fully automat...
متن کاملKnowledge-Based versus experimentally Acquired Distance and Angle Constraints for NMR Structure Refinement
Nuclear Overhauser effects (NOE) distance constraints and torsion angle constraints are major conformational constraints for nuclear magnetic resonance (NMR) structure refinement. In particular, the number of NOE constraints has been considered as an important determinant for the quality of NMR structures. Of course, the availability of torsion angle constraints is also critical for the formati...
متن کاملProtein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c.
A new approach to NMR solution structure refinement is introduced that uses paramagnetic effects on nuclear chemical shifts as constraints in energy minimization or molecular dynamics calculations. Chemical shift differences between oxidized and reduced forms of horse cytochrome c for more than 300 protons were used as constraints to refine the structure of the wild-type protein in solution and...
متن کاملNMR data-driven structure determination using NMR-I-TASSER in the CASD-NMR experiment.
NMR-I-TASSER, an adaption of the I-TASSER algorithm combining NMR data for protein structure determination, recently joined the second round of the CASD-NMR experiment. Unlike many molecular dynamics-based methods, NMR-I-TASSER takes a molecular replacement-like approach to the problem by first threading the target through the PDB to identify structural templates which are then used for iterati...
متن کاملProtein NMR Structures Refined without NOE Data
The refinement of low-quality structures is an important challenge in protein structure prediction. Many studies have been conducted on protein structure refinement; the refinement of structures derived from NMR spectroscopy has been especially intensively studied. In this study, we generated flat-bottom distance potential instead of NOE data because NOE data have ambiguity and uncertainty. The...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2015