From 4b5640353a8b3809a08cc84299344419210fa4b1 Mon Sep 17 00:00:00 2001 From: "W. Trevor King" Date: Thu, 25 Apr 2013 13:12:52 -0400 Subject: [PATCH] cantilever/theory.tex: Cite Walton 2008 as motivation --- src/cantilever/theory.tex | 19 ++++++++++++++++++- 1 file changed, 18 insertions(+), 1 deletion(-) diff --git a/src/cantilever/theory.tex b/src/cantilever/theory.tex index 386e2c7..a4a9a6c 100644 --- a/src/cantilever/theory.tex +++ b/src/cantilever/theory.tex @@ -1,4 +1,21 @@ -\section{Theory} +\section{Theoretical background} +\label{sec:cantilever:theory} + +Understanding a protein's free energy landscape is important to +effectively model protein folding and unfolding behavior. Force +spectroscopy has been a useful technique for exploring these free +energy landscapes and those of the related field of ligand-receptor +kinetics. In force spectroscopy with the atomic force microscope +(AFM), it is common practice to use spring constants in the range of +$50\U{pN/nm}$, but the effect of the cantilever itself on the free +energy landscape is generally ignored. However, in AFM +biotin-streptavidin unbinding experiments, \citet{walton08} +demonstrated a surprisingly strong effect on unbinding force due to +cantilever stiffness. The unbinding force approximately doubled due +to a change from a $35\U{pN/nm}$ cantilever to a $58\U{pN/nm}$ +cantilever. Alarmed by the magnitude of the shift, we repeated their +experiment on octomeric I27 to determine the magnitude for our +mechanical protein unfolding experiments. \begin{figure} \asyinclude{figures/schematic/landscape-cant} -- 2.26.2