NDLI: Force Spectroscopy of the Double-Tethered Concanavalin-A Mannose Bond

Content Provider	PubMed Central
Author	Ratto, Timothy V. Langry, Kevin C. Rudd, Robert E. Balhorn, Rodney L. Allen, Michael J. Mcelfresh, Michael W.
Copyright Year	2004
Abstract	We present the measurement of the force required to rupture a single protein-sugar bond using a methodology that provides selective discrimination between specific and nonspecific binding events and helps verify the presence of a single functional molecule on the atomic force microscopy tip. In particular, the interaction force between a polymer-tethered concanavalin-A protein (ConA) and a similarly tethered mannose carbohydrate was measured as 47 ± 9 pN at a bond loading rate of ∼10 nN/s. Computer simulations of the polymer molecular configurations were used to determine the angles that the polymers could sweep out during binding and, in conjunction with mass spectrometry, used to separate the angular effects from the effects due to a distribution of tether lengths. We find that when using commercially available polymer tethers that vary in length from 19 to 29 nm, the angular effects are relatively small and the rupture distributions are dominated by the 10-nm width of the tether length distribution. In all, we show that tethering both a protein and its ligand allows for the determination of the single-molecule bond rupture force with high sensitivity and includes some validation for the presence of a single-tethered functional molecule on the atomic force microscopy tip.
Related Links	http://dx.doi.org/10.1016/s0006-3495(04)74299-x
Ending Page	2437
Page Count	8
Starting Page	2430
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	4
Volume Number	86
Language	English
Publisher	Biophysical Society
Publisher Date	2004-04-01
Access Restriction	Open
Rights Holder	Biophysical Society
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

Probing molecular interaction between concanavalin A and mannose ligands by means of SFM

Hidden Multiple Bond Effects in Dynamic Force Spectroscopy

LexA-DNA Bond Strength by Single Molecule Force Spectroscopy

Effects of Multiple-Bond Ruptures on Kinetic Parameters Extracted from Force Spectroscopy Measurements: Revisiting Biotin-Streptavidin Interactions

Studying RecBCD Helicase Translocation Along χ-DNA Using Tethered Particle Motion with a Stretching Force

Dissimilar Kinetic Behavior of Electrically Manipulated Single- and Double-Stranded DNA Tethered to a Gold Surface

Force Generation by Actin Polymerization II: The Elastic Ratchet and Tethered Filaments

Contractile Fibers and Catch-Bond Clusters: a Biological Force Sensor?

The Force Exerted by a Muscle Cross-Bridge Depends Directly on the Strength of the Actomyosin Bond

Force Spectroscopy of the Double-Tethered Concanavalin-A Mannose Bond

Similar Documents

Probing molecular interaction between concanavalin A and mannose ligands by means of SFM

Hidden Multiple Bond Effects in Dynamic Force Spectroscopy

LexA-DNA Bond Strength by Single Molecule Force Spectroscopy

Effects of Multiple-Bond Ruptures on Kinetic Parameters Extracted from Force Spectroscopy Measurements: Revisiting Biotin-Streptavidin Interactions

Studying RecBCD Helicase Translocation Along χ-DNA Using Tethered Particle Motion with a Stretching Force

Dissimilar Kinetic Behavior of Electrically Manipulated Single- and Double-Stranded DNA Tethered to a Gold Surface

Force Generation by Actin Polymerization II: The Elastic Ratchet and Tethered Filaments

Contractile Fibers and Catch-Bond Clusters: a Biological Force Sensor?

The Force Exerted by a Muscle Cross-Bridge Depends Directly on the Strength of the Actomyosin Bond

Force Spectroscopy of the Double-Tethered Concanavalin-A Mannose Bond