Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance.
Explore this paper's citation graph
Summary
"Pseudo-structures" of the 20 common amino acid residues are introduced for use in protein spatial structure determinations, which rely on the use of intramolecular proton-proton distance constraints determined by nuclear Overhauser effects as input for distance geometry calculations.
- Type
- article
- Published
- 1983-10-05
- Cited by
- 846
- References
- 17
- OpenAlex
- https://openalex.org/W1964659291
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:25889382
Keywords
Intramolecular force, Proton, Chemistry, Resonance (particle physics), van der Waals force
References
- Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagon.
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations.
- NMR in biological research: Peptides and proteins
- Conformation of polypeptides and proteins.
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Glucagon bound to perdeuterated dodecylphosphocholine micelles.
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor.
- Computer simulation of protein folding
- Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation
- Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance.
- Heteronuclear vicinal coupling constants and site-specific isotopic substitution in the investigation of rotational isomerism in leucine
- Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance.
- High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface.
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OH
- The interpretation of protein structures: total volume, group volume distributions and packing density.
- Energy parameters in polypeptides. 8. Empirical potential energy algorithm for the conformational analysis of large molecules
- Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acids
- A simplified representation of protein conformations for rapid simulation of protein folding.
Cited by
- The solution structure of motilin from NMR distance constraints, distance geometry, molecular dynamics, and an iterative full relaxation matrix refinement.
- Conformation in solution of porcine brain natriuretic peptide determined by combined use of nuclear magnetic resonance and distance geometry.
- Time-averaged nuclear Overhauser effect distance restraints applied to tendamistat.
- Three-dimensional solution structure of the pleckstrin homology domain from dynamin.
- Validation of the use of intermolecular NOE constraints for obtaining docked structures of protein-ligand complexes
- The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa.
- Protein structure calculation from NMR data.
- Solution structure of αtα, a helical hairpin peptide of de novo design
- A cytoplasmic peptide of the neurotrophin receptor p75NTR: induction of apoptosis and NMR determined helical conformation
- Yeast Transcript Elongation Factor (TFIIS), Structure and Function
- Prion protein NMR structure and familial human spongiform encephalopathies.
- Lincomycin and clindamycin conformations. A fragment shared by macrolides, ketolides and lincosamides determined from TRNOE ribosome-bound conformations.
- Comparison of proto‐oncogenic and mutant forms of the transmembrane region of the Neu receptor in TFE
- Conformational analysis of human calcitonin in solution
- The Proprotein Convertase SKI-1/S1P
- SANE (Structure Assisted NOE Evaluation): An automated model-based approach for NOE assignment
- A Proline-Hinge Alters the Characteristics of the Amphipathic α-helical AMPs
- Geometric Algorithms for Protein Structure Determination Using Measurements From Nuclear Magnetic Resonance Spectroscopy
- Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR.
- Solution structure of the recombinant human oncoprotein p13MTCP1
Related papers
- A comparison of the intramolecular and intermolecular hydrogen bonding of N,N'-ethylenebis(aminobenzylidene) in the solid state with its salen analogue
- The X-Ray Structure of 5-Chlorosalicylaldehyde
- Switching between intermolecular and intramolecular reactions using flow microreactors: lithiation of 2-bromo-2′-silylbiphenyls
- Effect of intermolecular interactions on vibrational-energy transfer in the liquid phase
- Intermolecular Excimer Formation in Dinuclear Metal Complexes
- Competition between intermolecular and intramolecular association in flexible hard chain molecules
- Intermolecular and intramolecular hydrogen bonding in 5‐pyridylmethylenehydantoins: IR and NMR study
- Quantum-Chemical Insight Into Mechanism of Combined Intra-Intermolecular Cycloaddition
- Blue-shifted A-H stretching frequencies in complexes with methanol: the decisive role of intramolecular coupling.