Conformational significance of the intrachain disulfide linkages in immunoglobulins - Test2 - elhamkhani - TriplyDB

Conformational significance of the intrachain disulfide linkages in immunoglobulins

Conformational significance of the intrachain disulfide linkages in immunoglobulins

http://www.wikidata.org/entity/Q33707912

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Construction of a three-dimensional model of the polypeptide backbone of the variable region of kappa immunoglobulin light chains.An attempt to locate the non-helical and permissively helical sequences of proteins: application to the variable regions of immunoglobulin light and heavy chains.Independent folding of the variable and constant halves of a lambda immunoglobulin light chain.Differences in serum IgG structure in health and rheumatoid disease. Circular dichroism studies Using empirical phase diagrams to understand the role of intramolecular dynamics in immunoglobulin G stability The quaternary structure of amalgam, a Drosophila neuronal adhesion protein, explains its dual adhesion properties.The encephalitogenic protein of myelin forms hexamers in which the polypeptides have a pleated-sheet structure.

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P2860

Conformational significance of the intrachain disulfide linkages in immunoglobulins

http://www.wikidata.org/entity/Q33707912

description

1970 nî lūn-bûn

@nan

1970 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1970 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

1970年の論文

@ja

1970年論文

@yue

1970年論文

@zh-hant

1970年論文

@zh-hk

1970年論文

@zh-mo

1970年論文

@zh-tw

1970年论文

@wuu

name

Conformational significance of the intrachain disulfide linkages in immunoglobulins

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Conformational significance of the intrachain disulfide linkages in immunoglobulins

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type

label

Conformational significance of the intrachain disulfide linkages in immunoglobulins

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Conformational significance of the intrachain disulfide linkages in immunoglobulins

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prefLabel

Conformational significance of the intrachain disulfide linkages in immunoglobulins

@ast

Conformational significance of the intrachain disulfide linkages in immunoglobulins

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Conformational significance of the intrachain disulfide linkages in immunoglobulins

@en

P2093

Frommel D

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Good RA

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Litman GW

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Rosenberg A

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P2860

The complete amino acid sequence of Bence Jones protein Cum (kappa-type)

Subgroups of amino acid sequences in the variable regions of immunoglobulin heavy chains

Immunoglobulin lambda-chains. The complete amino acid sequence of a Bence-Jones protein

The complete amino acid sequence of Bence Jones protein New (lambda-type). Subgroups in the variable part of immunoglobulin L-chains of the lambda-type

[Chemical structure of 2 kappa-type Bence Jones proteins (Roy and Cum.)]

On the prevalence of "nonspecific" binding at the specific binding sites of globular proteins.

Comparison of invariant residues in the variable and constant regions of human K, human L, and mouse K Bence-Jones proteins.

The optical rotatory properties of the beta-configuration in polypeptides and proteins

On the location and structure of the active sites of antibody molecules.

Studies of the location of tyrosyl and tryptophyl residues in proteins. I. Solvent perturbation data of model compounds.

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1085-1092

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scholarly article

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10.1073/PNAS.67.3.1085

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3

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67

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1970-11-01T00:00:00Z

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283320

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