Literature DB >> 4337558

Homonuclear indor spectroscopy as a means of simplifying and analyzing proton magnetic resonance spectra of peptides and as a basis for determining secondary and tertiary conformations of complex peptides.

W A Gibbons, H Alms, R S Bockman, H R Wyssbrod.   

Abstract

Mesh：

Substances：

Year:  1972        PMID： 4337558     DOI： 10.1021/bi00759a030

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


× No keyword cloud information.
  4 in total

1.  The quantitation of nuclear Overhauser effect methods for total conformational analysis of peptides in solution. Application to gramicidin S.

Authors:  C R Jones; C T Sikakana; S Hehir; M C Kuo; W A Gibbons
Journal:  Biophys J       Date:  1978-12       Impact factor: 4.033

2.  Specificity of interproton nuclear Overhauser effects in gramicidin-S dissolved in deuterated ethylene glycol.

Authors:  A A Bothner-By; P E Johner
Journal:  Biophys J       Date:  1978-12       Impact factor: 4.033

3.  Amide hydrogen exchange rates of peptides in H2O solution by 1H nuclear magnetic resonance transfer of solvent saturation method. Conformations of oxytocin and lysine vasopressin in aqueous solution.

Authors:  N R Krishna; D H Huang; J D Glickson; R Rowan; R Walter
Journal:  Biophys J       Date:  1979-06       Impact factor: 4.033

4.  Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A.

Authors:  S Srimal; N Surolia; S Balasubramanian; A Surolia
Journal:  Biochem J       Date:  1996-04-15       Impact factor: 3.857
  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.