[PDF] Analysis Of The Precision And Accuracy Of Protein Structures Determined By Nmr eBook

Author :
Publisher :
Page : 161 pages
File Size : 34,48 MB
Release : 2006
Category :
ISBN :

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Nuclear magnetic resonance (NMR) has emerged as a powerful tool for determining three-dimensional structures of proteins in solution. The major part of this dissertation describes the efforts to deal with the core steps involved in NMR-base protein structure determination: NMR data collection, NMR data analysis, structure calculation and refinement. NMR data collection has been recognized as one of the major bottlenecks of NMR-base structure determination due to the necessarily long time. Chapter 2 and 3 describe two NMR data collection and analysis protocols for high-quality protein structure determination based on Reduced Dimensionality (RD) and G-matrix Fourier transform (GFT) NMR, respectively. The rapidly collected RD & GFT NMR data enabled high-quality structure determination of four structural genomics target proteins in high-throughput. Chapter 5 introduces the program UBNMR which was developed to facilitate NMR data analysis in general and RD & GFT NMR data pre-processing and data analysis in particular. RD and GFT NMR based protocols, with the aid of UBNMR, are expected to greatly impact on the NMR-based structural biology and structural genomics. In addition to rapid NMR data collection and analysis, structure calculation and refinement are also pivotal for obtaining the high-quality protein structures. Chapter 5 describes the analysis of the newly implemented simultaneous GFT NOESY to obtain an accurate and precise initial structural fold. Chapter 6 presents a protein structure refinement strategy using NOE data collected in supercooled water at low temperatures.

Author : John L. Markley
Publisher : Oxford University Press
Page : 375 pages
File Size : 11,74 MB
Release : 1997-01-30
Category : Science
ISBN : 0195357426

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This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Jardetsky, one of the pioneers of the field, is edited by two of the most highly respected investigators using NMR, and features contributions by most of the leading workers in the field. It will be valued as a landmark publication that presents the state-of-the-art perspectives regarding one of today's most important technologies.

Author : M. Zouhair Atassi
Publisher : Springer Science & Business Media
Page : 522 pages
File Size : 39,3 MB
Release : 2013-06-29
Category : Science
ISBN : 148991031X

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The MPSA international conference is held in a different country every two years. It is devoted to methods of determining protein structure with emphasis on chemistry and sequence analysis. Until the ninth conference, MPSA was an acronym for Methods in Protein Sequence Analysis. To give the conference more flexibility and breadth, the Scientific Advisory Committee of the lOth MPSA decided to change the name to Methods in Protein Structure Analysis; however, the emphasis remains on "methods" and on "chemistry. " In fact, this is the only major conference that is devoted to methods. The MPSA conference is truly international, a fact clearly reflected by the composi tion of its Scientific Advisory Committee. The Scientific Advisory Committee oversees the scientific direction of the MPSA and elects the chairman of the conference. Members of the committee are elected by active members, based on scientific standing and activity. The chairman, subject to approval of the Scientific Advisory Committee, appoints the Organizing Committee. It is this latter committee that puts the conference together. The lectures of the MPSA have traditionally been published in a special proceedings issue. This is different from, and more detailed than, the special MPSA issue of the Journal of Protein Chemistry in which only a brief description of the talks is given in short papers and abstracts. In the I Oth MPSA, about half the talks are by invited speakers and the remainder were selected from submitted short papers and abstracts.

Author : Kurt Wüthrich
Publisher : Wiley-Interscience
Page : 330 pages
File Size : 44,53 MB
Release : 1986
Category : Medical
ISBN :

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Lists of tables. The foundations: structure and NMR of biopolymers. Resonance assignments and structure determination in proteins. Resonance assignments and structure determiantion in nucleic acids. With NMR to biopolymer conformation and beyond.

Author : Kala Bharath Pilla
Publisher :
Page : 0 pages
File Size : 50,63 MB
Release : 2015
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Computational modelling of proteins that rely on either de novo or evolutionary based approaches often produce poor quality structures, primarily due to the limitations in their algorithms or forcefields. Traditional experimental techniques such as X-ray crystallography depend on narrow set of crystallographic conditions while solution/solid state nuclear magnetic resonance (NMR) spectroscopy relies on cumbersome spectral analysis and complete resonance assignments. These traditional approaches are slow and costly endeavours. Computational/experimental hybrid approaches on the other hand provide a new avenue for reliable, rapid and cost-effective structure determination. Paramagnetic NMR offers easy generation of useful and sparse structural information which can be implemented as restraints in structure prediction algorithms. Pseudocontact shifts (PCS) are the most powerful of structural restraints generated by paramagnetic NMR which are long range in nature and can be easily obtained by simple 2D NMR experiments. This thesis demonstrates different approaches involved in protein structure calculations using PCS restraints in Rosetta. Chapter 2 demonstrates structure determination using PCS restraints exclusively obtained from protein samples in microcrystalline state by magic angle spinning (MAS) NMR spectroscopy. Chapter 3 discusses the implementation of using PCS data from multiple metal centres to precisely determine the location of spins in space in a manner analogues to GPS-satellites. Chapter 4 extends the usage of PCS data from multiple metal centres to capture distinct conformational states in proteins. Chapter 5 demonstrates new techniques especially developed for structure determination of large proteins involving super secondary structure motifs (Smotifs) and data driven iterative resampling. These different computational techniques serve the goal of determining accurate 3D models using minimal experimental data, which are applicable to proteins systems that are currently beyond the realm of traditional experimental approaches.

Author : Wim Jiskoot
Publisher : Springer Science & Business Media
Page : 694 pages
File Size : 40,6 MB
Release : 2005-12-05
Category : Medical
ISBN : 9780971176720

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Protein pharmaceuticals form a fast-growing category in the arsenal of drugs. This book explores the nature of different analytical techniques and the way in which they are related to pharmaceutical proteins. In addition to serving the analytical chemist, this book is needed by the formulation scientist who is responsible for design and formulation of a pharmaceutical protein that can be monitored during production and over time.

Author : D.N. Rutledge
Publisher : Elsevier
Page : 567 pages
File Size : 38,92 MB
Release : 1996-06-10
Category : Science
ISBN : 0080541208

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Signal analysis and signal treatment are integral parts of all types of Nuclear Magnetic Resonance. In the last ten years, much has been achieved in the development of dimensional spectra. At the same time new NMR techniques such as NMR Imaging and multidimensional spectroscopy have appeared, requiring entirely new methods of signal analysis. Up until now, most NMR texts and reference books limited their presentation of signal processing to a short introduction to the principles of the Fourier Transform, signal convolution, apodisation and noise reduction. To understand the mathematics of the newer signal processing techniques, it was necessary to go back to the primary references in NMR, chemometrics and mathematics journals. The objective of this book is to fill this void by presenting, in a single volume, both the theory and applications of most of these new techniques to Time-Domain, Frequency-Domain and Space-Domain NMR signals. Details are provided on many of the algorithms used and a companion CD-ROM is also included which contains some of the computer programs, either as source code or in executable form. Although it is aimed primarily at NMR users in the medical, industrial and academic fields, it should also interest chemometricians and programmers working with other techniques.

Author : N. Rama Krishna
Publisher : Springer Science & Business Media
Page : 565 pages
File Size : 13,32 MB
Release : 2006-05-09
Category : Medical
ISBN : 0306470845

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Volume 17 is the second in a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series. Volume 16, with the subtitle Modern Techniques in Protein NMR , is the first in this series. These two volumes present some of the recent, significant advances in the biomolecular NMR field with emphasis on developments during the last five years. We are honored to have brought together in these volume some of the world s foremost experts who have provided broad leadership in advancing this field. Volume 16 contains - vances in two broad categories: I. Large Proteins, Complexes, and Membrane Proteins and II. Pulse Methods. Volume 17 contains major advances in: I. Com- tational Methods and II. Structure and Dynamics. The opening chapter of volume 17 starts with a consideration of some important aspects of modeling from spectroscopic and diffraction data by Wilfred van Gunsteren and his colleagues. The next two chapters deal with combined automated assignments and protein structure determination, an area of intense research in many laboratories since the traditional manual methods are often inadequate or laborious in handling large volumes of NMR data on large proteins. First, Werner Braun and his associates describe their experience with the NOAH/DIAMOD protocol developed in their laboratory.