文档介绍：NMR supplement
ic studies of protein folding using
NMR spectroscopy
Christopher M. Dobson and Peter J. Hore
Recent progress has advanced our abilities to use NMR spectroscopy to follow — in real time — the structural
and dynamic changes taking place during protein folding.
In a cell, the starting point of protein rant). This allows the use of biophysical polypeptide than there are molecules in
folding is the nascent chain as it forms techniques to follow the folding process the test tube. This means that the process
on the ribosome. The process of protein in real time. Two aspects of folding, how- of folding can involve extremely diverse
folding continues in a crowded molecu- ever, make this task challenging. The structural ensembles until the very last
lar environment, in the presence of a first is that folding is usually fast; many stages of the reaction. plicates
variety of helper molecules, the most small proteins fold in milliseconds or substantially the analysis of the results of
famous of which are the molecular chap- less, although others may take consider- structural studies.
erones whose major functions include ably longer. The second, and perhaps In order bat these problems,
the control of protein aggregation. Many most significant, is that the initial state one approach has been to utilize a wide
small proteins, however, will refold effi- from which