Christian B. Anfinsen

Inactivation of staphylococcal nuclease by the binding of antibodies to a distinct antigenic determinant

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTInactivation of staphylococcal nuclease by the binding of antibodies to a distinct antigenic determinantDavid H. Sachs, Alan N. Schec...

Principles that Govern the Folding of Protein Chains

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Acceleration of Reactivation of Reduced Bovine Pancreatic Ribonuclease by a Microsomal System from Rat Liver

Prior studies to this article by Anfinsen, Epstein, and Goldberger established that the time required for synthesizing a chain of protein such as ribonuclease in the tissues ...

The Genetic Control of Tertiary Protein Structure: Studies With Model Systems

At the present time it is generally assumed that most, if not all, proteins possess well-defined structures. This assumption is based on several kinds of evidence: (1) the findi...

Side-chain Interactions Governing the Pairing of Half-cystine Residues in Ribonuclease

Fully reduced ribonuclease (RNase), devoid of demonstrable secondary or tertiary structure, may be oxidized by molecular oxygen to yield a product which is indistinguishable by ...

Folding of staphylococcal nuclease: Kinetic studies of two processes in acid renaturation

Purification and Properties of an Enzyme from Beef Liver Which Catalyzes Sulfhydryl-Disulfide Interchange in Proteins

Abstract An enzyme which catalyzes sulfhydryl-disulfide interchange in proteins containing incorrect disulfide bonds has been isolated from beef liver microsomes. The purified f...

Studies on the Mechanism of the Enzymic Catalysis of Disulfide Interchange in Proteins

Abstract An enzyme that catalyzes disulfide interchange in proteins, localized in the microsomes of all tissues tested, has been isolated in pure form from bovine liver microsom...

Reconstitution of Fully Active RNase S by Carboxypeptidase-degraded RNase S-Peptide

Staphylococcal Nuclease (Foggi Strain)

Abstract The amino acid sequence of staphylococcal nuclease isolated from cultures of strain Foggi is presented. Except for some uncertainty concerning the states of amidation o...

A Solid Phase Synthetic Study of the Active Site Region of Staphylococcal Nuclease-T'

Abstract Solid phase synthetic peptides have been prepared corresponding to the sequence in staphylococcal nuclease of residues 6 through 47, as well as single substitution anal...

A Reinvestigation of the Sequence of Residues 11 to 18 in Bovine Pancreatic Ribonuclease

The Identification of Unreactive Amino Groups in Ribonuclease and Their Significance to Enzymatic Activity

Purification of Synthetic Ribonuclease S-Peptide Derivatives by Specific Complex Formation on Columns of Ribonuclease S-Protein Bound to Agarose

Abstract Ribonuclease S-protein was attached covalently to agarose which had been activated by treatment with cyanogen bromide according to the methods described by Porath and h...

Nonuniform Labeling of Egg White Lysozyme

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTNonuniform Labeling of Egg White LysozymeRobert E. Canfield and Christian B. AnfinsenCite this: Biochemistry 1963, 2, 5, 1073–1078Pub...

Synthetic Studies of Structure-Function Relationships in Staphylococcal Nuclease

Abstract The solid phase technique of peptide synthesis has been used to study structural features related to the activity of Fragment P2 (Residues 6 through 48) of nuclease-T. ...

Semisynthetic Analogues of an Enzymically Active Complex Formed between Two Overlapping Fragments of Staphylococcal Nuclease

Abstract It has been shown previously that a cyanogen bromide fragment of staphylococcal nuclease (149 residues) containing the COOH-terminal portion of the molecule (residues 9...