Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints.
نویسندگان
چکیده
0079-6565/$ see front matter Published by Elsevier doi:10.1016/j.pnmrs.2008.12.001 Abbreviations: NMR, Nuclear Magnetic Resonan RMSD, mean square deviation; HSQC, heteronuclea spectroscopy; NOE, Nuclear Overhauser Effect; RDC, re Protein Data Bank; pol g, zinc finger domain of the hu CH, C Ha; hSRI, human Set2-Rpb1 interacting do human transcription elongation factor CA150 (RN domain interacting protein); POF, principal order fram MD, molecular dynamics; SSE, secondary structure e WPS, well-packed satisfying; vdW, van der Waals; DO * Corresponding author. Tel.: +1 919 660 6583. E-mail address: [email protected] (B.R. D URL: http://www.cs.duke.edu/brd (B.R. Donald).
منابع مشابه
Robust structure-based resonance assignment for functional protein studies by NMR
High-throughput functional protein NMR studies, like protein interactions or dynamics, require an automated approach for the assignment of the protein backbone. With the availability of a growing number of protein 3D structures, a new class of automated approaches, called structure-based assignment, has been developed quite recently. Structure-based approaches use primarily NMR input data that ...
متن کاملAutomated protein fold determination using a minimal NMR constraint strategy.
Determination of precise and accurate protein structures by NMR generally requires weeks or even months to acquire and interpret all the necessary NMR data. However, even medium-accuracy fold information can often provide key clues about protein evolution and biochemical function(s). In this article we describe a largely automatic strategy for rapid determination of medium-accuracy protein back...
متن کاملThe fumarate sensor DcuS: progress in rapid protein fold elucidation by combining protein structure prediction methods with NMR spectroscopy.
We illustrate how moderate resolution protein structures can be rapidly obtained by interlinking computational prediction methodologies with un- or partially assigned NMR data. To facilitate the application of our recently described method of ranking and subsequent refining alternative structural models using unassigned NMR data [Proc. Natl. Acad. Sci. USA 100 (2003) 15404] for such "structural...
متن کاملA Polynomial-Time Algorithm for De Novo Protein Backbone Structure Determination from Nuclear Magnetic Resonance Data
We describe an efficient algorithm for protein backbone structure determination from solution Nuclear Magnetic Resonance (NMR) data. A key feature of our algorithm is that it finds the conformation and orientation of secondary structure elements as well as the global fold in polynomial time. This is the first polynomial-time algorithm for de novo high-resolution biomacromolecular structure dete...
متن کاملA dipolar coupling based strategy for simultaneous resonance assignment and structure determination of protein backbones.
A new approach for simultaneous protein backbone resonance assignment and structure determination by NMR is introduced. This approach relies on recent advances in high-resolution NMR spectroscopy that allow observation of anisotropic interactions, such as dipolar couplings, from proteins partially aligned in field ordered media. Residual dipolar couplings are used for both geometric information...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Progress in nuclear magnetic resonance spectroscopy
دوره 55 2 شماره
صفحات -
تاریخ انتشار 2009