Thermodynamic stability and kinetic stability of globular proteins.
نویسندگان
چکیده
منابع مشابه
Kinetic nonoptimality and vibrational stability of proteins.
Scaling of folding times in Go models of proteins and of decoy structures with the Lennard-Jones potentials in the native contacts reveal power law trends when studied under optimal folding conditions. The power law exponent depends on the type of native geometry. Its value indicates lack of kinetic optimality in the model proteins. In proteins, mechanical and thermodynamic stabilities are corr...
متن کاملThermodynamic stability of folded proteins against mutations
By balancing the average energy gap with its typical change due to mutations for protein-like heteropolymers with M residues, we show that native states are unstable to mutations on a scale M ∼ (λ/σμ) 1/ζs , where λ is the dispersion in the interaction free energies and σμ their typical change. Theoretical bounds and numerical estimates (based on complete enumeration on four lattices) of the in...
متن کاملThermodynamic stability and kinetic foldability of a lattice protein model.
By using serial mutations, i.e., a residue replaced by 19 kinds of naturally occurring residues, the stability of native conformation and folding behavior of mutated sequences are studied. The 3 x 3 x 3 lattice protein model with two kinds of interaction potentials between the residues, namely the original Miyazawa and Jernigan (MJ) potentials and the modified MJ potentials (MMJ), is used. Effe...
متن کاملThermodynamic stability versus kinetic lability of ZnS4 core.
Density Functional Theory and post-Hartree Fock calculations reveal an unusual energy profile for Zn-S and Zn-N bond dissociation reactions in several [Zn(SR)(4)](2-) and [Zn(Im)(SR)(3)](-) complexes. The Zn-S bond dissociation in tetrathiolate dianions, which is highly exothermic in the gas phase, proceeds through a late transition state which can be rationalized on the basis of an avoided cro...
متن کاملFormation and stability of secondary structures in globular proteins
We study two models for the formation and packing of helices and sheets in globular (compact) proteins. These models, based on weighted Hamiltonian paths on a regular lattice both exhibit a first order transition between a compact high temperature phase, with no extended secondary structures, and a quasi-frozen compact phase, with secondary structures invading the whole lattice. The quasi-froze...
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: Seibutsu Butsuri
سال: 1993
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.33.2