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Article

Thermodynamic effects of replacements of Pro residues in helix interiors of maltose-binding protein.

Proteins - 1 Dec 2003

Prajapati R S, Lingaraju G M, Bacchawat Kiran, Surolia Avadhesha, Varadarajan Raghavan

Abstract excerpt

Introduction of Pro residues into helix interiors results in protein destabilization. It is currently unclear if the converse substitution (i.e., replacement of Pro residues that naturally occur in helix interiors would be stabilizing). Maltose-binding protein is a large 370-amino acid protein that contains 21 Pro residues. Of these, three nonconserved residues (P48, P133, and P159) occur at helix interiors. Each...

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Source

Identifiers

PMID: 14635128
DOI: 10.1002/prot.10488

Genes

MBP

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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