Literature DB >> 4528456

Carbon-13 magnetic resonance evaluation of polypeptide secondary structure and correlation with proton magnetic resonance studies.

D W Urry, L W Mitchell, T Onishi.   

Abstract

With the use of appropriately chosen solvent pairs it is demonstrated that solvent dependence of peptide carbonyl carbon resonances can be correlated with polypeptide secondary structure. Solvent titrations show the peptide carbonyl which is intramolecularly hydrogen bonded to exhibit less chemical shift on going from a dimethylsulfoxide solution to a solution containing a solvent which is a good proton (or deuteron) donor. Effective solvent systems are dimethylsulfoxide paired with water, trifluoroethanol, or methanol. This approach is demonstrated with the pentapeptide of elastin.

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Year:  1974        PMID： 4528456      PMCID： PMC388665          DOI： 10.1073/pnas.71.8.3265

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN： 0027-8424            Impact factor:   11.205


  13 in total

1.  A carbon-13 nuclear magnetic resonance study of oxytocin and its oligopeptides.

Authors:  R Deslauriers; R Walter; I C Smith
Journal:  Biochem Biophys Res Commun       Date:  1972-08-21       Impact factor: 3.575

2.  Carbon-13 nuclear magnetic resonance spectroscopy of oxytocin, related oligopeptides, and selected analogs.

Authors:  A I Brewster; V J Hruby; A F Spatola; F A Bovey
Journal:  Biochemistry       Date:  1973-04-10       Impact factor: 3.162

3.  Proton magnetic resonance studies in trifluoroethanol. Solvent mixtures as a means of delineating peptide protons.

Authors:  T P Pitner; D W Urry
Journal:  J Am Chem Soc       Date:  1972-02-23       Impact factor: 15.419

4.  Prolactin synthesis in primates.

Authors:  A D Rudko; F M Lovell; B W Low
Journal:  Nat New Biol       Date:  1971-07-07

5.  The molecular structure and some transport properties of valinomycin.

Authors:  M Pinkerton; L K Steinrauf; P Dawkins
Journal:  Biochem Biophys Res Commun       Date:  1969-05-22       Impact factor: 3.575

6.  Temperature dependence of amide proton chemical shifts: the secondary structures of gramicidin S and valinomycin.

Authors:  M Ohnishi; D W Urry
Journal:  Biochem Biophys Res Commun       Date:  1969-07-23       Impact factor: 3.575

7.  A conformational analysis of gramicidin S-A by nuclear magnetic resonance.

Authors:  A Stern; W A Gibbons; L C Craig
Journal:  Proc Natl Acad Sci U S A       Date:  1968-10       Impact factor: 11.205

8.  Conformations of cyclic peptides. IV. Nuclear magnetic resonance studies of cyclo-pentaglycyl-L-leucyl and cyclo-diglycyl-L-histidyldiglycyl-L-tyrosyl.

Authors:  K D Kopple; M Ohnishi; A Go
Journal:  Biochemistry       Date:  1969-10       Impact factor: 3.162

9.  Secondary structure of the cyclic moiety of the peptide hormone oxytocin and its deamino analog.

Authors:  D W Urry; M Ohnishi; R Walter
Journal:  Proc Natl Acad Sci U S A       Date:  1970-05       Impact factor: 11.205

10.  Proposed conformation of oxytocin in solution.

Authors:  D W Urry; R Walter
Journal:  Proc Natl Acad Sci U S A       Date:  1971-05       Impact factor: 11.205
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  3 in total

1.  Conformation of sequential polypeptide poly(Leu-Leu-D-Phe-Pro) and formation of ion channel across bilayer lipid membrane.

Authors:  J Kamegai; S Kimura; Y Imanishi
Journal:  Biophys J       Date:  1986-05       Impact factor: 4.033

2.  Conformational and receptor-binding properties of the insect neuropeptide proctolin and its analogues.

Authors:  B Odell; S J Hammond; R Osborne; M W Goosey
Journal:  J Comput Aided Mol Des       Date:  1996-04       Impact factor: 3.686

3.  'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG.

Authors:  G Merutka; H J Dyson; P E Wright
Journal:  J Biomol NMR       Date:  1995-01       Impact factor: 2.835
  3 in total

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