Buried and Accessible Surface Area Control Intrinsic Protein Flexibility
نویسندگان
چکیده
منابع مشابه
Buried and accessible surface area control intrinsic protein flexibility.
Proteins experience a wide variety of conformational dynamics that can be crucial for facilitating their diverse functions. How is the intrinsic flexibility required for these motions encoded in their three-dimensional structures? Here, the overall flexibility of a protein is demonstrated to be tightly coupled to the total amount of surface area buried within its fold. A simple proxy for this, ...
متن کاملProtein flexibility and intrinsic disorder.
Comparisons were made among four categories of protein flexibility: (1) low-B-factor ordered regions, (2) high-B-factor ordered regions, (3) short disordered regions, and (4) long disordered regions. Amino acid compositions of the four categories were found to be significantly different from each other, with high-B-factor ordered and short disordered regions being the most similar pair. The hig...
متن کاملProtein-protein interactions: general trends in the relationship between binding affinity and interfacial buried surface area.
Protein-protein interactions play key roles in many cellular processes and their affinities and specificities are finely tuned to the functions they perform. Here, we present a study on the relationship between binding affinity and the size and chemical nature of protein-protein interfaces. Our analysis focuses on heterodimers and includes curated structural and thermodynamic data for 113 compl...
متن کاملPacking efficiency and accessible surface area of crumpled graphene
Steven W. Cranford and Markus J. Buehler* Center for Materials Science and Engineering, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts, USA and Department of Civil and Environmental Engineering, Laboratory of Atomistic and Molecular Mechanics, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Room 1-235A&B, Cambridge, Massachusetts, 02139 ...
متن کاملSolvent accessible surface area approximations for rapid and accurate protein structure prediction
The burial of hydrophobic amino acids in the protein core is a driving force in protein folding. The extent to which an amino acid interacts with the solvent and the protein core is naturally proportional to the surface area exposed to these environments. However, an accurate calculation of the solvent-accessible surface area (SASA), a geometric measure of this exposure, is numerically demandin...
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: Journal of Molecular Biology
سال: 2013
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2013.06.019