Secondary structure and unfolding of wild-type ribonuclease T1 and mutants that affect enzyme catalysis - a fourier transform infrared spectroscopic study

DOIResolve DOI: http://doi.org/10.1007/978-94-011-1934-4_129
AuthorSearch for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for: ; Search for:
TypeBook Chapter
Proceedings titleFifth International Conference on the Spectroscopy of Biological Molecules
ConferenceThe 5th European Conference on the Spectroscopy of Biological Molecules (ECSBM), September 5-10, 1993, Loutraki, Greece
ISBN978-94-010-4855-2
978-94-011-1934-4
Pages361364; # of pages: 4
AbstractRibonuclease T1 (RNase T1) is a small globular enzyme composed of 104 amino acids. Its three-dimensional structure is known and genetically-engineered overproducers are available (for a review see Ref. 1), which makes RNase T1 an excellent model system for investigating several aspects of protein folding. Various X-ray studies have shown that the secondary structure of RNase T1 includes a long α-helix, a major antiparallel β-sheet composed of three long and two short β-strands, a short two-stranded antiparallel β-sheet close to the N-terminus of the protein, and four wide loops which include several types of turns (Fig. 1).
Publication date
PublisherKluwer Academic
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biodiagnostics
Peer reviewedNo
NRC number316
NPARC number9742761
Export citationExport as RIS
Report a correctionReport a correction
Record identifierf84c3d03-f9d7-4f38-a3ce-db86bac5efc4
Record created2009-07-17
Record modified2016-12-12
Bookmark and share
  • Share this page with Facebook (Opens in a new window)
  • Share this page with Twitter (Opens in a new window)
  • Share this page with Google+ (Opens in a new window)
  • Share this page with Delicious (Opens in a new window)