Pages that link to "Q79403316"
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The following pages link to Side-chain interactions governing the pairing of half-cystine residues in ribonuclease (Q79403316):
Displaying 32 items.
- The protein folding problem (Q28284812) (← links)
- Selective inactivation of guanine-nucleotide-binding regulatory protein (G-protein) alpha and betagamma subunits by urea (Q28348354) (← links)
- Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding (Q30987192) (← links)
- Techniques for the analysis of cysteine sulfhydryls and oxidative protein folding. (Q33828281) (← links)
- Protein Folding at the Exit Tunnel (Q34168308) (← links)
- RECOVERY OF ANTIGENIC SPECIFICITY AFTER DENATURATION AND COMPLETE REDUCTION OF DISULFIDES IN A PAPAIN FRAGMENT OF ANTIBODY (Q34415237) (← links)
- Scaling properties of glycine-rich sequences in guanidine hydrochloride solutions (Q35895144) (← links)
- DISULFIDE INTERCHANGE AND THE THREE-DIMENSIONAL STRUCTURE OF PROTEINS (Q36015937) (← links)
- Refolding of misfolded mutant GPCR: post-translational pharmacoperone action in vitro (Q36316416) (← links)
- Conformational differences between the biologically active and inactive forms of a transfer ribonucleic acid (Q36463732) (← links)
- Protein folding in membranes. (Q37681352) (← links)
- Stability of protein pharmaceuticals (Q38734028) (← links)
- Problems in Protein Biosynthesis (Q40048842) (← links)
- Implication of the structure and stability of disulfide intermediates of lysozyme on the mechanism of renaturation (Q40336821) (← links)
- UV resonance Raman studies of the NaClO4 dependence of poly-L-lysine conformation and hydrogen exchange kinetics (Q40685954) (← links)
- Mia40 is a facile oxidant of unfolded reduced proteins but shows minimal isomerase activity (Q40899371) (← links)
- Tryptophan stabilizes His-heme loops in the denatured state only when it is near a loop end (Q41917991) (← links)
- Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate (Q42112518) (← links)
- Quantitation of the nearest-neighbour effects of amino acid side-chains that restrict conformational freedom of the polypeptide chain using reversed-phase liquid chromatography of synthetic model peptides with L- and D-amino acid substitutions (Q42114239) (← links)
- Controlling the speed of hirudin folding (Q42160965) (← links)
- Localization and some properties of skin sulfhydryl oxidase (Q42523053) (← links)
- Ultraviolet Resonance Raman Study of Side Chain Electrostatic Control of Poly-l-Lysine Conformation (Q42712429) (← links)
- Apo-azurin folds via an intermediate that resembles the molten-globule (Q43105013) (← links)
- Hydrogen bonds are a primary driving force for de novo protein folding. (Q47130583) (← links)
- Unearthing the root of amino acid similarity. (Q50929972) (← links)
- [Chemical synthesis of proteins]. (Q53776274) (← links)
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis (Q64244254) (← links)
- Effect of oxidative sulfitolysis of disulfide bonds of bovine serum albumin on its structural properties: a physiochemical study (Q68086009) (← links)
- Unfolding the Mysteries of Protein Metamorphosis (Q88771240) (← links)
- A look back at the molten globule state of proteins: thermodynamic aspects (Q91765309) (← links)
- Structure-Function Relationships in Ribonuclease S: the Work of Frederic M. Richards (Q93485919) (← links)
- Enhancing our Understanding of Protein Structure: the Work of Jane and David Richardson (Q93527179) (← links)