Literature DB >> 4508315

Nuclear magnetic resonance determination of the angle psi in peptides.

S Karplus, M Karplus.   

Abstract

A simple theoretical model is used to suggest that the NCCH coupling constant, Jnh, has a dihedral angle dependence that can serve for estimating the angle Psi in peptides. Some experimental comparisons are made to test the model; they include a new measurement of Jnh in N-acetylglycine.

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Year:  1972        PMID： 4508315      PMCID： PMC389736          DOI： 10.1073/pnas.69.11.3204

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


  3 in total

1.  Variation of the NH-C alpha-H coupling constant with dihedral angle in the NMR spectra of peptides.

Authors:  G N Ramachandran; R Chandrasekaran; K D Kopple
Journal:  Biopolymers       Date:  1971-11       Impact factor: 2.505

2.  Conformational studies of peptide systems. The rotational states of the NH--CH fragment of alanine dipeptides by nuclear magnetic resonance.

Authors:  V F Bystrov; S L Portnova; V I Tsetlin; V T Ivanov; Y A Ovchinnikov
Journal:  Tetrahedron       Date:  1969-02       Impact factor: 2.457

3.  Solution conformation of ferrichrome, a microbial iron transport cyclohexapeptide, as deduced by high resolution proton magnetic resonance.

Authors:  M Llinás; M P Klein; J B Neilands
Journal:  J Mol Biol       Date:  1970-09-28       Impact factor: 5.469
  3 in total
  1 in total

1.  Application of the primary hydration shell approach to locally enhanced sampling simulated annealing: computer simulation of thyrotropin-releasing hormone in water.

Authors:  A Rosenhouse-Dantsker; R Osman
Journal:  Biophys J       Date:  2000-07       Impact factor: 4.033
  1 in total

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