Literature DB >> 4735791

Temperature variation of polyribonucleotide conformation by an interaction with basic globular proteins.

D A Stevenson, J W Preiss.   

Abstract

Chicken lysozyme interacts with polyribonucleotides to form large light-scattering centers. The size of these is critically dependent on conformation of the polynucleotides. Hence, the interaction provides a very sensitive method of determining temperature intervals within which the polynucleotides change from multistranded, stacked-base structures to single-stranded, random coils. This change can be observed with the unaided eye, especially when concentrations of polynucleotides are of the order of a few micrograms per milliliter.

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Year:  1973        PMID: 4735791      PMCID: PMC1484303          DOI: 10.1016/S0006-3495(73)86000-X

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  3 in total

1.  The complexing of lysozyme with poly C and other homopolymers.

Authors:  J W Preiss
Journal:  Biophys J       Date:  1968-11       Impact factor: 4.033

2.  Pancreatic ribonuclease-poly G complexes: complete inhibition of poly U hydrolysis.

Authors:  J W Preiss; J A Sands
Journal:  Biophys J       Date:  1969-10       Impact factor: 4.033

3.  Some parallelisms n the behavior of pancreatic ribonuclease and chicken lysozyme toward homopolyribonucleotides.

Authors:  J W Preiss; D A Stevenson
Journal:  Biophys J       Date:  1972-01       Impact factor: 4.033

  3 in total

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