(Q53993518)

English

Contribution of the intramolecular disulfide bridge to the folding stability of REIv, the variable domain of a human immunoglobulin kappa light chain.

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scholarly article

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Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Contribution of the intramolecular disulfide bridge to the folding stability of REIv, the variable domain of a human immunoglobulin kappa light chain. (English)

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

6

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Thomas Schneider

8

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

author name string

Frisch C

1

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Kolmar H

2

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Schmidt A

3

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Kleemann G

4

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Reinhardt A

5

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Usón I

7

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Fritz HJ

9

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

publication date

1 January 1996

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Folding & design

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

1

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

6

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

431-440

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

Diversity of the immunoglobulin gene superfamily

1 reference

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Three-Dimensional Structure of Immunoglobulins

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Man-made antibodies

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Equilibrium and kinetics of the denaturation of a homogeneous human immunoglobulin light chain

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The Role of the Intrachain Disulfide Bond in the Conformation and Stability of the Constant Fragment of the Immunoglobulin Light Chain1

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Mono‐ and Bivalent Antibody Fragments Produced in Escherichia coli: Engineering, Folding and Antigen Binding

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The disulfide bonds in antibody variable domains: effects on stability, folding in vitro, and functional expression in Escherichia coli.

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Sequence statistics reliably predict stabilizing mutations in a protein domain

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General mutagenesis/gene expression procedure for the construction of variant immunoglobulin domains in Escherichia coli. Production of the Bence-Jones protein REIv via fusion to beta-lactamase

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Molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-Å resolution

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Dimerization of Bence Jones proteins: linking the rate of transcription from an Escherichia coli promoter to the association constant of REIV.

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Additivity of mutational effects in proteins

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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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Conformation of the constant fragment of the immunoglobulin light chain: effect of cleavage of the polypeptide chain and the disulfide bond

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Measuring and increasing protein stability

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Enthalpic destabilization of a mutant human lysozyme lacking a disulfide bridge between cysteine-77 and cysteine-95

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Unfolding and refolding of the reduced constant fragment of the immunoglobulin light chain. Kinetic role of the intrachain disulfide bond

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7 January 2021

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The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability

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Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature

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Identifiers

10.1016/S1359-0278(96)00059-4

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 May 2018

http://europepmc.org/abstract/MED/9080189

ResearchGate publication ID

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