NDLI: Measurement of intercolumnar forces between parallel guanosine four-stranded helices.

Content Provider	PubMed Central
Author	Mariani, P. Saturni, L.
Abstract	The deoxyguanosine-5'-monophosphate in aqueous solution self-associates into stable structures, which include hexagonal and cholesteric columnar phases. The structural unit is a four-stranded helix, composed of a stacked array of Hoogsteen-bonded guanosine quartets. We have measured by osmotic stress method the force per unit length versus interaxial distance between helices in the hexagonal phase under various ionic conditions. Two contributions have been recognized: the first one is purely electrostatic, is effective at large distances, and shows a strong dependence on the salt concentration of the solution. The second contribution is short range, dominates at interaxial separations smaller than about 30-32 A, and rises steeply as the columns approach each other, preventing the coalescence of the helices. This repulsion has an exponential nature and shows a magnitude and a decay length insensitive to the ionic strength of the medium. Because these features are distinctive of the hydration force detected between phospholipid bilayers or between several linear macromolecules (DNA, polysaccharides, collagen), we conclude that the dominant force experienced by deoxyguanosine helices approaching contact is hydration repulsion. The observed decay length of about 0.7 A has been rationalized to emerge from the coupling between the 3-A decay length of water solvent and the helically ordered structure of the hydrophilic groups on the opposing surfaces. The present results agree with recent measurements, also showing the dependence of the hydration force decay on the structure of interacting surfaces and confirm the correlations between force and structure.
Related Links	http://dx.doi.org/10.1016/s0006-3495(96)79856-9
Ending Page	2874
Page Count	8
Starting Page	2867
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	6
Volume Number	70
Language	English
Publisher Date	1996-06-01
Access Restriction	Open
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Helix-specific interactions induce condensation of guanosine four-stranded helices in concentrated salt solutions.

Direct measurement of temperature-dependent solvation forces between DNA double helices.

Direct measurement of the intermolecular forces between counterion-condensed DNA double helices. Evidence for long range attractive hydration forces.

Measurement of the repulsive force between polyelectrolyte molecules in ionic solution: hydration forces between parallel DNA double helices.

A molecular model for RecA-promoted strand exchange via parallel triple-stranded helices.

Attractive Forces between Cation Condensed DNA Double Helices

Hydration forces between parallel DNA double helices: computer simulations.

Direct measurement of forces between self-assembled proteins: temperature-dependent exponential forces between collagen triple helices.

Folds induced by multiple parallel or antiparallel double-helices: (pseudo)knotting of single-stranded RNA

Measurement of intercolumnar forces between parallel guanosine four-stranded helices.

Similar Documents

Helix-specific interactions induce condensation of guanosine four-stranded helices in concentrated salt solutions.

Direct measurement of temperature-dependent solvation forces between DNA double helices.

Direct measurement of the intermolecular forces between counterion-condensed DNA double helices. Evidence for long range attractive hydration forces.

Measurement of the repulsive force between polyelectrolyte molecules in ionic solution: hydration forces between parallel DNA double helices.

A molecular model for RecA-promoted strand exchange via parallel triple-stranded helices.

Attractive Forces between Cation Condensed DNA Double Helices

Hydration forces between parallel DNA double helices: computer simulations.

Direct measurement of forces between self-assembled proteins: temperature-dependent exponential forces between collagen triple helices.

Folds induced by multiple parallel or antiparallel double-helices: (pseudo)knotting of single-stranded RNA

Measurement of intercolumnar forces between parallel guanosine four-stranded helices.