Ontology highlight
ABSTRACT:
SUBMITTER: Ghosh A
PROVIDER: S-EPMC4317052 | biostudies-literature | 2014 Jul
REPOSITORIES: biostudies-literature
Ghosh Ayanjeet A Tucker Matthew J MJ Gai Feng F
The journal of physical chemistry. B 20140418 28
It is well known that histidine is involved in many biological functions due to the structural versatility of its side chain. However, probing the conformational transitions of histidine in proteins, especially those occurring on an ultrafast time scale, is difficult. Herein we show, using a histidine dipeptide as a model, that it is possible to probe the tautomer and protonation status of a histidine residue by measuring the two-dimensional infrared (2D IR) spectrum of its amide I vibrational t ...[more]