(Q71045293)

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Folding of homologous proteins. The refolding of different ribonucleases is independent of sequence variations, proline content and glycosylation

scientific article published on 01 September 1983

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scholarly article

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15 October 2019

Folding of homologous proteins. The refolding of different ribonucleases is independent of sequence variations, proline content and glycosylation (English)

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15 October 2019

author name string

H Krebs

1

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15 October 2019

F X Schmid

2

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15 October 2019

R Jaenicke

3

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publication date

1 September 1983

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15 October 2019

Journal of Molecular Biology

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15 October 2019

169

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15 October 2019

619-635

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15 October 2019

2

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15 October 2019

Binding of phosphate ligands to ribonuclease A

1 reference

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An examination of the involvement of proline peptide isomerization in protein folding

1 reference

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The molecular evolution of pancreatic ribonuclease

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues

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Kinetic study of protein unfolding and refolding using urea gradient electrophoresis

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Characterization of the slow steps in the folding of the alpha subunit of tryptophan synthase

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Spectrophotometric assay of bovine pancreatic ribonuclease by the use of cytidine 2':3'-phosphate

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Relation between Structure and Function in Some Partially Synthetic Ribonucleases S'. Enzymic and Spectroscopic Investigation on [Orn10,Asn14]-RNase S' and 1e,7e, 10delta-Triguanidino-[Orn10, Asn14]-R Nase S'

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Unfolding and refolding of the constant fragment of the immunoglobulin light chain

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Kinetic analysis of the reversible folding reactions of small proteins: Application to the folding of lysozyme and cytochrome c

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A quantitative treatment of the kinetics of the folding transition of ribonuclease A

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Transmembrane assembly of membrane and secretory glycoproteins

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Kinetic Evidence for Incorrectly Folded Intermediate States in the Refolding of Denatured Proteins

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Kinetics of unfolding and refolding of proteins. I. Mathematical analysis.

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The role of proline residues in the folding kinetics of the bovine pancreatic trypsin inhibitor derivative RCAM(14–38)

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Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme

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Identification and characterization of the direct folding process of hen egg-white lysozyme

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Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding

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Invariant features of the structure of pancreatic ribonuclease. A test of different predictive models

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Effect of proline residues on protein folding

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Further evidence suggesting that the slow phase in protein unfolding and refolding is due to proline isomerization: a kinetic study of carp parvalbumins

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Isomerization of proline-93 during the unfolding and refolding of ribonuclease A

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Swine pepsinogen folding intermediates are highly structured, motile molecules

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Guanidine hydrochloride induced unfolding of yeast iso-2 cytochrome c

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Reinvestigation of the primary structures of red deer and roe deer pancreatic ribonuclease and proline sites in mammalian ribonucleases

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7 January 2021

Nature of the fast and slow refolding reactions of iron(III) cytochrome c

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The properties of bovine pancreatic ribonuclease in ethylene glycol solution

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The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentration

1 reference

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7 January 2021

Proline peptide isomerization and the reactivation of denatured enzymes

1 reference

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7 January 2021

Kinetics of unfolding and refolding of proteins. 3. Results for lysozyme

1 reference

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7 January 2021

The primary structure of goat and sheep pancreatic ribonucleases

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7 January 2021

Determination of Serum Glycoproteins

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The yield of reactivation of lactic dehydrogenase after guanidine HCl denaturation is not determined by proline cis in equilibrium trans isomerization

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Amino-acid sequences of red-deer and roe-deer pancreatic ribonucleases

1 reference

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Relaxation spectrometry of biological systems

1 reference

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based on heuristic

inferred from DOI database lookup

A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A

1 reference

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7 January 2021

based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/S0022-2836(83)80067-9

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6620387%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6620387%20AND%20SRC:MED&resulttype=core&format=json

15 October 2019

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