Home LiteratureArticle Details

PMID: 7688608 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions.

Annual review of biophysics and biomolecular structure ·Vol. 22 ·1993-00-00 ·Pages 123-42

Schmid FX

Abstract

暂无摘要

MeSH Terms

Amino Acid Isomerases/chemistry,metabolism Amino Acid Sequence Carrier Proteins/chemistry,metabolism Catalysis Humans Kinetics Models, Structural Molecular Sequence Data Oligopeptides/chemistry Peptidylprolyl Isomerase Protein Folding Protein Structure, Secondary Ribonuclease T1/chemistry Tacrolimus/metabolism Tacrolimus Binding Proteins

Chemicals

Carrier Proteins Oligopeptides Ribonuclease T1 Amino Acid Isomerases Tacrolimus Binding Proteins Peptidylprolyl Isomerase Tacrolimus

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Schmid F X

Laboratorium für Biochemie, Universität Bayreuth, Germany.

Article Info

Journal

Annual review of biophysics and biomolecular structure

Abbr.

Annu Rev Biophys Biomol Struct

ISSN

1056-8700

DOI

10.1146/annurev.bb.22.060193.001011

Published

1993-00-00

Pages

123-42

Language

English

Region

United States

NLM ID

9211097

Subset

External Links

PubMed source DOI: 10.1146/annurev.bb.22.060193.001011

Analysis Services

Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions.

Contact

WeChat Official Account