Conformation in solution of porcine brain natriuretic peptide determined by combined use of nuclear magnetic resonance and distance geometry.
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Summary
The conformation in solution of porcine brain natriuretic peptide was determined by combined use of NMR spectroscopy and distance geometry using a set of 157 inter-proton-distance constraints derived from the two-dimensional NOE spectra and three hydrogen bond constraints obtained from analysis of the temperature dependence of labile protons.
- Type
- article
- Published
- 1990-10-01
- Cited by
- 11
- References
- 35
- Access
- Open access
- OpenAlex
- https://openalex.org/W2146114
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:29207333
Keywords
Computer science
References
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- Further Studies on the Use of Multi-substituted Benzenesulfonyl Groups for Protection of the Guanidino Function of Arginine
- Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm.
- The conformation of alpha-human atrial natriuretic polypeptide in solution.
- Molecular dynamics simulation techniques for determination of molecular structures from nuclear magnetic resonance data.
- 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.
- Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance.
- A new natriuretic peptide in porcine brain
- Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry.
- Conformations of cyclic peptides. IV. Nuclear magnetic resonance studies of cyclo-pentaglycyl-L-leucyl and cyclo-diglycyl-L-histidyldiglycyl-L-tyrosyl.
- Two‐Dimensional NMR studies of [Pro‐10] atrial natriuretic factor [7‐23]
- Improved spectral resolution in cosy 1H NMR spectra of proteins via double quantum filtering.
- Transition structures for additions of lithium hydride and methyllithium to ethylene and acetylene
- Structural basis of hierarchical multiple substates of a protein. IV: Rearrangements in atom packing and local deformations
- Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance.
- NMR study of the solution conformation of rat atrial natriuretic factor 7-23 in sodium dodecyl sulfate micelles.
- Structural basis of hierarchical multiple substates of a protein. V: Nonlocal deformations
- Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases
Cited by
- Pituitary adenylate cyclase activating polypeptide (PACAP) with 27 residues. Conformation determined by 1H NMR and CD spectroscopies and distance geometry in 25% methanol solution.
- 1H-NMR studies of the natriuretic peptide urodilatin: sequence-specific resonance assignment.
- The endocrine heart and natriuretic peptides: histochemistry, cell biology, and functional aspects of the renal urodilatin system
- Evaluation of conformational and binding characteristics of various natriuretic peptides and related analogs.
- Natriuretic peptide drug leads from snake venom.
- Functional and structural characterization of a novel member of the natriuretic family of peptides from the venom of Pseudocerastes persicus
- Conformations of platypus venom C-type natriuretic peptide in aqueous solution and sodium dodecyl sulfate micelles.
- The conformation of porcine-brain natriuretic peptide by two-dimensional NMR spectroscopy.
- Hydrophobic forces are responsible for the folding of a highly potent natriuretic peptide analogue at a membrane mimetic surface: an NMR study.
- Taipan Natriuretic Peptides Are Potent and Selective Agonists for the Natriuretic Peptide Receptor A
- The Biochemistry of Atrial Natriuretic Peptides
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