Pages that link to "Q44411649"
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The following pages link to Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitor (Q44411649):
Displaying 50 items.
- Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor (Q21045382) (← links)
- Molecular structures of glycoprotein hormones and functions of their carbohydrate components (Q24528086) (← links)
- The anatomy and taxonomy of protein structure (Q28277011) (← links)
- From Levinthal to pathways to funnels (Q28300934) (← links)
- Protein unfolding during reversed-phase chromatography: I. Effect of surface properties and duration of adsorption (Q30308120) (← links)
- Polypeptide chain folding through a highly helical intermediate as a general principle of globular protein structure formation (Q30413467) (← links)
- Hydrogen exchange in BPTI variants that do not share a common disulfide bond (Q30416869) (← links)
- Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor (Q31054951) (← links)
- Toward a better understanding of protein folding pathways (Q33631849) (← links)
- A conformational isomer of bovine pancreatic trypsin inhibitor protein produced by refolding (Q34286496) (← links)
- Toward an understanding of the folding of ribonuclease A. (Q34338750) (← links)
- Conformations of intermediates in the folding of the pancreatic trypsin inhibitor (Q34398571) (← links)
- Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic trypsin inhibitor (Q34601857) (← links)
- What the papers say: Protein folding pathways determined using disulphide bonds (Q35174815) (← links)
- Protein folding guides disulfide bond formation (Q36056772) (← links)
- Mutational analysis of the BPTI folding pathway: I. Effects of aromatic → leucine substitutions on the distribution of folding intermediates (Q36280455) (← links)
- Mutational analysis of the BPTI folding pathway: II. Effects of aromatic → leucine substitutions on folding kinetics and thermodynamics (Q36280506) (← links)
- Regeneration of RNase A from the reduced protein: models of regeneration pathways (Q36313092) (← links)
- The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor (Q37120974) (← links)
- Kinetic role of nonnative species in the folding of bovine pancreatic trypsin inhibitor (Q37257578) (← links)
- Minimal models for proteins and RNA from folding to function (Q37361859) (← links)
- Genetic analysis of the folding pathway for the tail spike protein of phage P22 (Q37507965) (← links)
- Early steps in the refolding reaction of reduced ribonuclease A (Q39186079) (← links)
- Stability of proteins: small globular proteins (Q39303667) (← links)
- Experimental studies of protein folding and unfolding (Q39772419) (← links)
- Unfolding thermodynamics of cysteine-rich proteins and molecular thermal-adaptation of marine ciliates (Q39871888) (← links)
- Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation (Q40336821) (← links)
- Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI). (Q41020151) (← links)
- The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. (Q41065191) (← links)
- Protein folding coupled to disulphide bond formation (Q41648380) (← links)
- Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein (Q41762447) (← links)
- Early intermediates in the PDI-assisted folding of ribonuclease A (Q42198037) (← links)
- Genetic Selection for Enhanced FoldingIn VivoTargets the Cys14-Cys38 Disulfide Bond in Bovine Pancreatic Trypsin Inhibitor (Q42627750) (← links)
- Comparison of solution structures of mutant bovine pancreatic trypsin inhibitor proteins using two‐dimensional nuclear magnetic resonance (Q42841815) (← links)
- Modeling the role of disulfide bonds in protein folding: Entropic barriers and pathways (Q54085346) (← links)
- Secretion incompetence of bovine pancreatic trypsin inhibitor expressed in Escherichia coli (Q54700465) (← links)
- BPTI folding revisited: switching a disulfide into methylene thioacetal reveals a previously hidden path. (Q55283783) (← links)
- Prediction of protein structure from amino acid sequence (Q56881117) (← links)
- Nature's transitory covalent bond (Q57961189) (← links)
- A peptide model of a protein folding intermediate (Q59073101) (← links)
- Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase (Q60066033) (← links)
- Refolding of bovine trypsinogen with one and two disulfide bonds reduced and carboxymethylated (Q67019141) (← links)
- Refolding of bovine pancreatic trypsin inhibitor modified at methionine-52 (Q67319167) (← links)
- Reductive cleavage and regeneration of the disulfide bonds inStreptomyces subtilisin inhibitor (SSI) as studied by the carbonyl13C NMR resonances of cysteinyl residues (Q67908757) (← links)
- Local interactions favor the native 8-residue disulfide loop in the oxidation of a fragment corresponding to the sequence Ser-50-Met-79 derived from bovine pancreatic ribonuclease A (Q68086005) (← links)
- Residues cys-1 and cys-79 are not essential for refolding of reduced-denatured kringle 4 fragment of human plasminogen (Q70217270) (← links)
- The Influence of Effectors on the Refolding (Reactivation) of Immobilized Trypsin (Q70760036) (← links)
- The role of proline residues in the folding kinetics of the bovine pancreatic trypsin inhibitor derivative RCAM(14–38) (Q70879791) (← links)
- Refolding of S-methylmethionyl basic pancreatic trypsin inhibitor (Q70879876) (← links)
- A three-disulphide intermediate in refolding of reduced ribonuclease A with a folded conformation (Q71330258) (← links)