Results 1 - 10
of
84,579
Applications of molecular modelling in NMR structure determination
"... Structure determination by liquid state NMR has emerged as a structure deter-mination technique for macromolecules only 13 years ago. From the beginning, molecular modelling has had a central place in the derivation of NMR solution structures [1–4]. This has several reasons. First, the energy parame ..."
Abstract
-
Cited by 1 (0 self)
- Add to MetaCart
Structure determination by liquid state NMR has emerged as a structure deter-mination technique for macromolecules only 13 years ago. From the beginning, molecular modelling has had a central place in the derivation of NMR solution structures [1–4]. This has several reasons. First, the energy
Solid-State NMR Structure Determination of Melittin in a
"... All in-text references underlined in blue are linked to publications on ResearchGate, letting you access and read them immediately. ..."
Abstract
- Add to MetaCart
All in-text references underlined in blue are linked to publications on ResearchGate, letting you access and read them immediately.
NMR Structure Determination for Larger Proteins Using Backbone-Only Data
"... Conventional protein structure determination from nuclear magnetic resonance data relies heavily on side-chain proton-proton distances. The necessary side-chain resonance assignment, however, is labor intensive and prone to error. Here we show that structures can be accurately determined without NMR ..."
Abstract
-
Cited by 32 (0 self)
- Add to MetaCart
for proteins greater than 15 kDa, and should enable routine NMR structure determination for larger proteins. The first step in protein structure determination by NMR is chemical shift assignment for the backbone atoms. In contrast to the subsequent assignment of the sidechains, this is now
Protein NMR Structure Determination with Automated NOE Assignment Using the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA
- J. Mol. Biol
, 2002
"... Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE crosspeak assignment and protein structure ..."
Abstract
-
Cited by 148 (10 self)
- Add to MetaCart
Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE crosspeak assignment and protein
Crystallography & NMR system: A new software suite for macromolecular structure determination.
- Acta Crystallogr. D Biol. Crystallogr.
, 1998
"... Abstract A new software suite, called Crystallography & NMR System (CNS), has been developed for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy. In contrast to existing structure determination programs the architecture o ..."
Abstract
-
Cited by 1411 (6 self)
- Add to MetaCart
Abstract A new software suite, called Crystallography & NMR System (CNS), has been developed for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy. In contrast to existing structure determination programs the architecture
Magic Angle Spinning NMR Structure Determination of Proteins from Pseudocontact Shifts
"... ABSTRACT: Magic angle spinning solid-state NMR is a unique technique to study atomic-resolution structure of biomacromole-cules which resist crystallization or are too large to study by solution NMR techniques. However, difficulties in obtaining sufficient number of long-range distance restraints us ..."
Abstract
- Add to MetaCart
using dipolar coupling based spectra hamper the process of structure determination of proteins in solid-state NMR. In this study it is shown that high-resolution structure of proteins in solid phase can be determined without the use of traditional dipolar−dipolar coupling based distance restraints
Limits of NMR structure determination using variable target function calculations: ribonuclease TI, a case
- Subcetl. Biochem.: Proteins - Structure, finction, and Engineering
, 1997
"... Limits of NMR structure determination using multidimensional NMR spectroscopy, variable target function calculations and relaxation matrix analysis were explored using the model protein ribonuclease T1 (RNase T1). The enzyme consists of 104 amino acid residues and has a molecular mass of approximate ..."
Abstract
-
Cited by 9 (0 self)
- Add to MetaCart
Limits of NMR structure determination using multidimensional NMR spectroscopy, variable target function calculations and relaxation matrix analysis were explored using the model protein ribonuclease T1 (RNase T1). The enzyme consists of 104 amino acid residues and has a molecular mass
1 SUPPLEMENTARY MATERIAL FOR: Accurate automated protein NMR structure determination using unassigned NOESY data
"... Materials and methods Protein expression, cloning, and purification All proteins used for the study were expressed, cloned and purified based on the Northeast Structural Genomics Consortium (NESG) standard methodologies previously published. 1 Briefly, constructs for ARI3A_HUMAN residues 218-351 and ..."
Abstract
- Add to MetaCart
required for NMR structure determination were fermented using ( 15 NH4)2SO4 and U- 13 C-glucose as the sole sources of nitrogen and carbon, respectively.
Results 1 - 10
of
84,579