(Q39212237)

10 September 2017

Refolding transition of α-chymotrypsin: pH and salt dependence (English)

1 reference

29 March 2022

Refolding transition of alpha-chymotrypsin: pH and salt dependence (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A29661

29 March 2022

1 reference

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A29661

29 March 2022

1 reference

29 March 2022

author name string

J. D. Stoesz

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A29661

29 March 2022

R. W. Lumry

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A29661

29 March 2022

language of work or name

English

0 references

publication date

1 September 1978

1 reference

10 September 2017

5 September 1978

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=29661

full work available at URL

29 March 2022

https://pubs.acs.org/doi/pdf/10.1021/bi00611a003

1 reference

29 March 2022

1 reference

10 September 2017

17

1 reference

10 September 2017

18

1 reference

10 September 2017

3693-3699

1 reference

Dimerization of alpha-chymotrypsin. II. Ionic strength and temperature dependence

10 September 2017

1

10

1617

Auné K. C.

1971

1 reference

On the interaction of the active side of alpha-chymotrypsin with chromophores: proflavin binding and enzyme conformation during catalysis

29 March 2022

3

18

405

Bernhard S. A.

1966

1 reference

I. Serine proteinases. The structure of alpha-chymotrypsin

29 March 2022

5

257

67

Birktoft J. J.

1970

1 reference

Succinylation of the amino group of isoleucine 16 in delta-chymotrypsin with retention of activity

29 March 2022

6

14

86

Blair T. T.

1971

1 reference

Physicochemical investigation of the chymotrypsins. II. On the mechanism of dimerization of chymotrypsin

29 March 2022

11

66

366

Egan R.

1957

1 reference

Conformational equilibria in -and -chymotrypsin. The energetics and importance of the salt bridge

29 March 2022

13

64

497

Fersht A. R.

1972

1 reference

Chymotrypsinogen: 2,5-Å crystal structure, comparison with α-chymotrypsin, and implications for zymogen activation

29 March 2022

15

9

1997

Freer S. T.

1970

1 reference

Binding interactions between two ligands and a monomeric protein. Study on indole, protons and chymotrypsin

29 March 2022

16

47

41

Garel J. R.

1970

1 reference

Activity and conformation of the alkaline form of δ-chymotrypsin studied by the specific acylation of isoleucine-16

29 March 2022

17

9

3902

Ghelis C.

1970

1 reference

Studies of the activity of chymotrypsin.

29 March 2022

21

257

89

Hess G. P.

1970

1 reference

Prototropic equilibrium of the reaction of diisopropylphosphofluoridate with α-chymotrypsin

29 March 2022

series ordinal

25

0 references

Asymmetrical changes in the tertiary structure of alpha-chymotrypsin with change in pH.

27

13

3661

Mavridis A.

1974

1 reference

Conformation of the high pH form of chymotrypsin

29 March 2022

28

39

551

McConn J.

1969

1 reference

Sedimentation of chemically modified chymotrypsin

29 March 2022

30

136

223

Neet K. E.

1970

1 reference

Control of conformation of α-chymotrypsin through chemical modification

29 March 2022

38

12

2933

Taylor R. P.

1973

1 reference

Variability in the tertiary structure of α-chymotrypsin at 2.8-Å resolution

29 March 2022

39

12

4185

Tulinsky A.

1973

1 reference

29 March 2022

Identifiers

DOI

10.1021/BI00611A003

1 reference

10 September 2017

1 reference