Pages that link to "Q72607100"

The following pages link to A native tertiary interaction stabilizes the A state of cytochrome c (Q72607100):

Displaying 42 items.

• The 40s Omega-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c (Q28289534) (← links)
• A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding (Q28365672) (← links)
• van't Hoff enthalpies without baselines. (Q30327076) (← links)
• Insights into the role of the histidines in the structure and stability of cytochrome c. (Q30352041) (← links)
• Collapse and cooperativity in protein folding (Q30424224) (← links)
• Protein folding: the endgame (Q30427987) (← links)
• Role of the molten globule state in protein folding. (Q33883824) (← links)
• Protein folding: matching theory and experiment (Q34168466) (← links)
• Effect of D57N mutation on membrane activity and molecular unfolding of cobra cardiotoxin (Q34169357) (← links)
• Selective excitation of native fluctuations during thermal unfolding simulations: horse heart cytochrome c as a case study (Q34180662) (← links)
• The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding (Q35646586) (← links)
• Mutational analysis of the BPTI folding pathway: II. Effects of aromatic → leucine substitutions on folding kinetics and thermodynamics (Q36280506) (← links)
• Identification of kinetically hot residues in proteins (Q36280778) (← links)
• Hydrophobic sequence minimization of the alpha-lactalbumin molten globule (Q36810158) (← links)
• Requirements for perpendicular helix pairing (Q36828221) (← links)
• Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region (Q37493928) (← links)
• The role of key residues in structure, function, and stability of cytochrome-c. (Q38101468) (← links)
• On-pathway versus off-pathway folding intermediates (Q41394280) (← links)
• Exploring the cytochrome c folding mechanism: cytochrome c552 from thermus thermophilus folds through an on-pathway intermediate (Q42169209) (← links)
• Equilibrium unfolding of a small low-potential cytochrome, cytochrome c553 from Desulfovibrio vulgaris (Q42847160) (← links)
• Denaturant mediated unfolding of both native and molten globule states of maltose binding protein are accompanied by large deltaCp's (Q42847238) (← links)
• Extended cardiolipin anchorage to cytochrome c: a model for protein-mitochondrial membrane binding (Q43125478) (← links)
• Sequential unfolding of the two-domain protein Pseudomonas stutzeri cytochrome c(4). (Q43919692) (← links)
• Glycerol-induced formation of the molten globule from acid-denatured cytochrome c: implication for hierarchical folding (Q43922613) (← links)
• Conformational states of trifluoroacetic acid-treated cytochrome c in the presence of salts and alcohols (Q44938817) (← links)
• A single mutation induces molten globule formation and a drastic destabilization of wild-type cytochrome c at pH 6.0. (Q46092446) (← links)
• A stable, molten-globule-like cytochrome c. (Q46315300) (← links)
• Anion concentration modulates the conformation and stability of the molten globule of cytochrome c. (Q47910982) (← links)
• The phage lambda terminase enzyme: 1. Reconstitution of the holoenzyme from the individual subunits enhances the thermal stability of the small subunit (Q47917290) (← links)
• Native-like secondary structure of molten globules. (Q52047122) (← links)
• A study of the influence of the hydrophobic core residues of yeast iso-2-cytochrome c on phosphate binding: a probe of the hydrophobic core-surface charge interactions. (Q52054903) (← links)
• Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology. (Q52520638) (← links)
• pH Dependence of Structural and Functional Properties of Oxidized Cytochromec" fromMethylophilus methylotrophus (Q57997905) (← links)
• Packing interactions in the apomyglobin folding intermediate (Q71031209) (← links)
• How molten is the molten globule? (Q71116533) (← links)
• Watching protein folding unfold (Q71726921) (← links)
• Kinetic intermediates in the formation of the cytochrome c molten globule (Q71840986) (← links)
• Direct electrochemical evidence for an equilibrium intermediate in the guanidine-induced unfolding of cytochrome c (Q71844006) (← links)
• Formation of a molten-globule-like state of cytochrome c induced by high concentrations of glycerol (Q73006506) (← links)
• Effect of dextran on protein stability and conformation attributed to macromolecular crowding (Q73009406) (← links)
• Kinetic role of early intermediates in protein folding (Q73070815) (← links)
• Is the manganese stabilizing 33 kDa protein of photosystem II attaining a 'natively unfolded' or 'molten globule' structure in solution? (Q73450401) (← links)