Loop-closure principles in protein folding.
نویسنده
چکیده
Simple theoretical concepts and models have been helpful to understand the folding rates and routes of single-domain proteins. As reviewed in this article, a physical principle that appears to underly these models is loop closure.
منابع مشابه
Loop-closure events during protein folding: rationalizing the shape of Phi-value distributions.
In the past years, the folding kinetics of many small single-domain proteins has been characterized by mutational Phi-value analysis. In this article, a simple, essentially parameter-free model is introduced which derives folding routes from native structures by minimizing the entropic loop-closure cost during folding. The model predicts characteristic folding sequences of structural elements s...
متن کاملHydrogen-Bond Driven Loop-Closure Kinetics in Unfolded Polypeptide Chains
Characterization of the length dependence of end-to-end loop-closure kinetics in unfolded polypeptide chains provides an understanding of early steps in protein folding. Here, loop-closure in poly-glycine-serine peptides is investigated by combining single-molecule fluorescence spectroscopy with molecular dynamics simulation. For chains containing more than 10 peptide bonds loop-closing rate co...
متن کاملUsing loop length variants to dissect the folding pathway of a four-helix-bundle protein.
Rop is a four-helix-bundle protein formed by the association of two helix-loop-helix monomers. The short helix-connecting loop was replaced with a series of polyglycine linkers of increasing length. These mutant proteins all appear to fold via the same general mechanism as that of the wild-type protein, even at the longest loop lengths. Replacement of the wild-type two-residue loop (Asp-Ala) wi...
متن کاملAn inverse correlation between loop length and stability in a four-helix-bundle protein.
BACKGROUND The loops in proteins are less well characterized than the secondary structural elements that they connect. We have used the four-helix-bundle protein Rop as a model system in which to explore the role of loop length in protein folding and stability. RESULTS A natural two-residue loop was replaced with a series of glycine linkers up to 10 residues in length. All 10 mutants are high...
متن کاملCooperativity in two-state protein folding kinetics.
We present a solvable model that predicts the folding kinetics of two-state proteins from their native structures. The model is based on conditional chain entropies. It assumes that folding processes are dominated by small-loop closure events that can be inferred from native structures. For CI2, the src SH3 domain, TNfn3, and protein L, the model reproduces two-state kinetics, and it predicts w...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Archives of biochemistry and biophysics
دوره 469 1 شماره
صفحات -
تاریخ انتشار 2008