about
Structural heterogeneity of the various forms of apomyoglobin: implications for protein foldingHigh stability of a ferredoxin from the hyperthermophilic archaeon A. ambivalens: involvement of electrostatic interactions and cofactorsMembrane-induced changes in the holomyoglobin tertiary structure: interplay with function.Protein folding observed by time-resolved synchrotron x-ray scattering. A feasibility studyConformational substates and motions in myoglobin. External influences on structure and dynamics.High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.Cold denaturation and 2H2O stabilization of a staphylococcal nuclease mutant.UV resonance Raman determination of molecular mechanism of poly(N-isopropylacrylamide) volume phase transition.Cold denaturation of staphylococcal nucleaseTemperature dependence of histidine ionization constants in myoglobinNegative activation enthalpies in the kinetics of protein folding.Highly anomalous energetics of protein cold denaturation linked to folding-unfolding kineticsDifferences in the processes of beta-lactoglobulin cold and heat denaturationsCold instability of aponeocarzinostatin and its stabilization by labile chromophore.Anaerobic storage of red blood cells.Fast photochemical oxidation of proteins and mass spectrometry follow submillisecond protein folding at the amino-acid level.Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate stateCold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognitionGeneration and Characterization of Environmentally Sensitive Variants of the beta-Galactosidase from Lactobacillus delbrueckii subsp. bulgaricus.Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation.Thermodynamics of BPTI foldingCrevice-forming mutants of bovine pancreatic trypsin inhibitor: stability changes and new hydrophobic surfaceThermal denaturation of iso-1-cytochrome c variants: comparison with solvent denaturation.Conformational properties of native sperm whale apomyoglobin in solution.Structure and dynamics of the water around myoglobinMechanical stability of helical beta-peptides and a comparison of explicit and implicit solvent models.Protein stability during freezing: separation of stresses and mechanisms of protein stabilization.Beyond water activity: recent advances based on an alternative approach to the assessment of food quality and safety.Computing protein stabilities from their chain lengths.Prediction of the thermodynamics of protein unfolding: the helix-coil transition of poly(L-alanine).Protein stability: electrostatics and compact denatured states.Direct observation of fast protein folding: the initial collapse of apomyoglobin.Enhancing uniformity and overall quality of red cell concentrate with anaerobic storage.Cold denaturation of proteins.Role of water in the formation of macromolecular structures.Cold denaturation of monoclonal antibodies.Calorimetric studies of the kinetic unfreezing of molecular motions in hydrated lysozyme, hemoglobin, and myoglobinPressure-induced subunit dissociation and unfolding of dimeric beta-lactoglobulin.Thermodynamics of interactions between amino acid side chains: experimental differentiation of aromatic-aromatic, aromatic-aliphatic, and aliphatic-aliphatic side-chain interactions in water.Pathways in two-state protein folding.
P2860
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P2860
description
1986 nî lūn-bûn
@nan
1986 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
Cold denaturation of myoglobin.
@ast
Cold denaturation of myoglobin.
@en
type
label
Cold denaturation of myoglobin.
@ast
Cold denaturation of myoglobin.
@en
prefLabel
Cold denaturation of myoglobin.
@ast
Cold denaturation of myoglobin.
@en
P2093
P1476
Cold denaturation of myoglobin.
@en
P2093
Kutyshenko VP
Privalov PL
Venyaminov SYu
P304
P356
10.1016/0022-2836(86)90017-3
P407
P577
1986-08-01T00:00:00Z