Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.
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Summary
A set of conformational restraints derived from nuclear magnetic resonance (n.m.r.) measurements on solutions of the basic pancreatic trypsin inhibitor (BPTI) was used as input for distance geometry calculations with the programs DISGEO and DISMAN and it is clear that the protein architecture observed in single crystals of BPTI is largely preserved in aqueous solution.
- Type
- article
- Published
- 1987-08-05
- Cited by
- 525
- References
- 41
- OpenAlex
- https://openalex.org/W1548025383
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:25857393
Keywords
Radius of gyration, Nuclear Overhauser effect, Geometry, Gyration, Crystallography
References
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- Theory and applications of distance geometry
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- Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm.
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- 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.
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- Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance.
- Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry.
- The theory and practice of distance geometry
- NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor
- Combined suppression of diagonal peaks and t1 ridges in two-dimensional nuclear overhauser enhancement spectra
- Some uses of a best molecular fit routine
- The internal dynamics of globular proteins.
- Spatial arrangement of the three α helices in the solution conformation of E. coli lac represser DNA‐binding domain
- Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances.
Cited by
- Stereospecific assignment of β-methylene protons in larger proteins using 3D15N-separated Hartmann-Hahn and13C-separated rotating frame Overhauser spectroscopy
- 1H and 15N assignments and secondary structure of the PI3K SH3 domain
- Solution structure of αtα, a helical hairpin peptide of de novo design
- Yeast Transcript Elongation Factor (TFIIS), Structure and Function
- Proton nuclear magnetic resonance assignments.
- The structural basis of Edc3‐ and Scd6‐mediated activation of the Dcp1:Dcp2 mRNA decapping complex
- Helix Nucleation by the Smallest Known α-Helix in Water.
- Conformational flexibility in calcitonin: The dynamic properties of human and salmon calcitonin in solution
- Identification of a Conserved N-Capping Box Important for the Structural Autonomy of the Prion α3-Helix: The Disease Associated D202N Mutation Destabilizes the Helical Conformation
- Increased Resolution of Aromatic Cross Peaks Using Alternate 13C Labeling and TROSY
- Spin labeling of proteins.
- Error analysis of macromolecular structures determined with nuclear magnetic resonance data.
- Recent developments in enzyme and microbial biotechnology--strategies in bioprocess design.
- Deuteration in protein proton magnetic resonance.
- Three-dimensional structure in solution of a wheat lipid-transfer protein from multidimensional 1H-NMR data. A new folding for lipid carriers.
- Solution structures of two zinc-finger domains from SWI5 obtained using two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger structure with a third strand of beta-sheet.
- Novel topology of a zinc‐binding domain from a protein involved in regulating early Xenopus development.
- Lipases and esterases: a review of their sequences, structure and evolution.
- Three-dimensional solution structure of an insulin dimer
- Three‐dimensional NMR structure of the sixth ligand‐binding module of the human LDL receptor: comparison of two adjacent modules with different ligand binding specificities
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