Hydrogen exchange: A sensitive analytical window into protein conformation and dynamics

TY - CHAP

T1 - Hydrogen exchange

T2 - A sensitive analytical window into protein conformation and dynamics

AU - Jensen, Pernille Foged

AU - Rand, Kasper Dyrberg

PY - 2016/3

Y1 - 2016/3

N2 - Hydrogen exchange (HX) monitored by mass spectrometry (MS) is a powerful analytical method for investigation of protein conformation and dynamics. HX-MS monitors isotopic exchange of hydrogen in protein backbone amides and thus serves as a sensitive method for probing protein conformation and dynamics along the entire protein backbone. This chapter describes the exchange of backbone amide hydrogen which is highly quenchable as it is strongly dependent on the pH and temperature. The HX rates of backbone amide hydrogen are sensitive and very useful probes of protein conformation, as they are distributed along the polypeptide backbone and form the fundamental hydrogen-bonding networks of basic secondary structure. The effect of pressure on HX in unstructured polypeptides (poly-dl-lysine and oxidatively unfolded ribonuclease A) and native folded proteins (lysozyme and ribonuclease A) was evaluated by Carter et al. The HX rate at high pressure was enhanced for both unstructured polypeptides and for folded proteins.

AB - Hydrogen exchange (HX) monitored by mass spectrometry (MS) is a powerful analytical method for investigation of protein conformation and dynamics. HX-MS monitors isotopic exchange of hydrogen in protein backbone amides and thus serves as a sensitive method for probing protein conformation and dynamics along the entire protein backbone. This chapter describes the exchange of backbone amide hydrogen which is highly quenchable as it is strongly dependent on the pH and temperature. The HX rates of backbone amide hydrogen are sensitive and very useful probes of protein conformation, as they are distributed along the polypeptide backbone and form the fundamental hydrogen-bonding networks of basic secondary structure. The effect of pressure on HX in unstructured polypeptides (poly-dl-lysine and oxidatively unfolded ribonuclease A) and native folded proteins (lysozyme and ribonuclease A) was evaluated by Carter et al. The HX rate at high pressure was enhanced for both unstructured polypeptides and for folded proteins.

UR - http://eu.wiley.com/WileyCDA/WileyTitle/productCd-1118616499.html

M3 - Book chapter

SN - 978-1-118-61649-9

SP - 1

EP - 17

BT - Hydrogen Exchange Mass Spectrometry of protein

A2 - Weis, David

PB - Wiley

ER -