Initiation sites of protein folding by NMR analysis.
نویسندگان
چکیده
منابع مشابه
Initiation sites of protein folding by NMR analysis.
Detailed characterization of denatured states of proteins is necessary to understand the interactions that funnel the large number of possible conformations along fast routes for folding. Nuclear magnetic resonance experiments based on the nuclear Overhauser effect (NOE) detect hydrogen atoms close in space and provide information about local structure. Here we present an NMR procedure that det...
متن کاملMillisecond protein folding studied by NMR spectroscopy.
Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecond-to-millisecond time scale. Together with an overview of current a...
متن کاملIdentification of initiation sites for T4 lysozyme folding using CD and NMR spectroscopy of peptide fragments.
Using CD and 2D (1)H NMR spectroscopy, we have identified potential initiation sites for the folding of T4 lysozyme by examining the conformational preferences of peptide fragments corresponding to regions of secondary structure. CD spectropolarimetry showed most peptides were unstructured in water, but adopted partial helical conformations in TFE and SDS solution. This was also consistent with...
متن کاملNMR studies of protein folding
NMR spectroscopy is the method of choice for determining the structural details of unfolded and partially folded states of proteins. Here, the utility of NMR spectroscopy in characterizing such disordered states which populate protein folding pathways, is discussed. The relevance of the structural information obtained to protein folding mechanisms is examined critically. NMR spectroscopy can no...
متن کاملDetection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis.
A simple alternative method for obtaining "random coil" chemical shifts by intrinsic referencing using the protein's own peptide sequence is presented. These intrinsic random coil backbone shifts were then used to calculate secondary chemical shifts, that provide important information on the residual secondary structure elements in the acid-denatured state of an acyl-coenzyme A binding protein....
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1996
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.93.20.10600