منابع مشابه
Structural Insight into RNA Hairpin Folding Intermediates
Hairpins are a ubiquitous secondary structure motif in RNA molecules. Despite their simple structure, there is some debate over whether they fold in a two-state or multi-state manner. We have studied the folding of a small tetraloop hairpin using a serial version of replica exchange molecular dynamics on a distributed computing environment. On the basis of these simulations, we have identified ...
متن کاملCharacterizing protein folding intermediates.
To determine the pathway by which a protein folds up, it is necessary to characterize the structures of folding intermediates and also to place these intermediates in the correct order on the kinetic pathway of folding. Noncovalent folding reactions are fast: typically they occur in seconds or less for small single-domain proteins. On the other hand, hours are required to obtain detailed struct...
متن کاملKinetic and equilibrium folding intermediates.
Our recent experiments on the molten globule state and other protein folding intermediates lead to following conclusions: (i) the molten globule is separated by intramolecular first-order phase transitions from the native and unfolded states and therefore is a specific thermodynamic state of protein molecules; (ii) the novel equilibrium folding intermediate (the 'pre-molten globule' state) exis...
متن کاملKinetic and equilibrium folding intermediates
O u r recent experim ents on the m olten globule state and o ther protein folding in term ediates lead to following conclusions: (i) the m olten globule is separated by in tram olecular first-order phase transitions from the native and unfolded states and therefore is a specific therm odynam ic state of protein molecules; (ii) the novel equilibrium folding in term ediate (the ‘pre-m olten g lob...
متن کاملStructural Characteristics of Stable Folding Intermediates of Yeast Iso-1-Cytochrome-c
Cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. More than 280 sequences have been reported in the protein sequence database (www.uniprot.org). Though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. Thus a vast data set of varied sequences with retention of similar structure and fun...
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: Annual Review of Biophysics
سال: 2010
ISSN: 1936-122X,1936-1238
DOI: 10.1146/annurev.biophys.093008.131334