ArticleBiophysical journal2007
Conformational dynamics in loop swap mutants of homologous fibronectin type III domains.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Effective harmonic potentials: insights into the internal cooperativity and sequence-specificity of protein dynamics.PLoS computational biology · 2013Article
- Exposing the Moving Parts of Proteins with NMR Spectroscopy.The journal of physical chemistry letters · 2012Article
- AMP-activated protein kinase β-subunit requires internal motion for optimal carbohydrate binding.Biophysical journal · 2012Article
- Chimeric fibronectin matrix mimetic as a functional growth- and migration-promoting adhesive substrate.Biomaterials · 2011Article
- The flexibility of a distant loop modulates active site motion and product release in ribonuclease A.Biochemistry · 2009Article
- Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase.Biochemistry · 2009Article
- Transient opening of fibronectin type III (FNIII) domains: the interaction of the third FNIII domain of FN with anastellin.Biochemistry · 2009Article
- Protein conformational flexibility prediction using machine learning.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
- Structure and dynamics of Ca2+-binding domain 1 of the Na+/Ca2+ exchanger in the presence and in the absence of Ca2+.Journal of molecular biology · 2008Article
- Crosstalk between the protein surface and hydrophobic core in a core-swapped fibronectin type III domain.Journal of molecular biology · 2008Article
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Authors and funding
3 authors.
Funding
Abstract
Fibronectin type III (FN-III) domains are autonomously folded modules found in a variety of multidomain proteins. The 10th FN-III domain from fibronectin (fnFN10) and the 3rd FN-III domain from tenascin-C (tnFN3) have 27% sequence identity and the same overall fold; however, the CC' loop has a different pattern of backbone hydrogen bonds and the FG loop is longer in fnFN10 compared to tnFN3. To examine the influence of length, sequence, and context in determining dynamical properties of loops, CC' and FG loops were swapped between fnFN10 and tnFN3 to generate four mutant proteins and backbone conformational dynamics on ps-ns and mus-ms timescales were characterized by solution (15)N-NMR spin relaxation spectroscopy. The grafted loops do not strongly perturb the properties of the protein scaffold; however, specific effects of the mutations are observed for amino acids that are proximal in space to the sites of mutation. The amino acid sequence primarily dictates conformational dynamics when the wild-type and grafted loop have the same length, but both sequence and context contribute to conformational dynamics when the loop lengths differ. The results suggest that changes in conformational dynamics of mutant proteins must be considered in both theoretical studies and protein design efforts.
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