Cited by 98Protein Structure and DynamicsPancreatic function and diabetesChemical Synthesis and Analysis

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Conformation of glucagon. Predictions and consequences

Chou, Peter Y., Fasman, Gerald D.·1975·Biochemistry

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Abstract

It is proposed that glucagon, a polypeptide hormone, is delicately balanced between two major conformational states. Utilizing a new predictive model [Chou, P.Y., and Fasman, G.D. (1974), Biochemistry 13, 222] which considers all the conformational states in proteins (helix, beta sheet, random coil, and beta turns), the secondary structural regions of glucagon are computed herein. The conformational sensitivity of glucagon may be due to residues 19-27 which have both alpha-helical potential (mean value of Palpha = 1.19) as well as beta-sheet potential (mean value of Pbeta = 1.25). Two conformational states are predicted for glucagon. In predicted form (a), residues 5-10 form a beta-sheet region while residues 19-27 form an alpha-helical region (31% alpha, 21% beta) agreeing well with the circular dichroism (CD) spectra of glucagon. The similarity in the CD spectra of glucagon and insulin further suggests the presence of beta structure in glucagon, since X-ray analysis of insulin showed 24% beta sheet. In predicted form (b), both regions, residues 5-10 and residues 19-27, are beta sheets sheets (0% alpha, 52% beta) in agreement with the infrared spectral evidence that glucagon gels and fibrils have a predominant beta-sheet conformation. Since three reverse beta turns are predicted at residues 2-5, 10-13, and 15-18, glucagon may possess tertiary structure in agreement with viscosity and tritium-hydrogen exchange experiments. A proposal is offered concerning an induced alpha yields beta transition at residues 22-27 in glucagon during receptor site binding. Amino acid substitutions are proposed which should disrupt the beta sheets of glucagon with concomitant loss of biological activity. The experimental findings that glucagon aggregates to form dimers, trimers, and hexamers can be explained in terms of beta-sheet interactions as outlined in the present predictive model. Thus the conflicting conclusions of previous workers, concerning the conformation of glucagon in different environments, can be rationalized by the suggested conformational transition occurring within the molecule.

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Santoro, A., Macis, M., Buonocore, M., et al. (2026) · Protein Science · doi:10.1002/pro.70750
Proton NMR Studies of the Active Centre of ACTH
Toma, F., Dive, V., Lőw, M., & KISFALUDY, L. (1986) · Birkhäuser Boston eBooks · doi:10.1007/978-1-4615-8521-3_11

Authors: Chou, P. Y., & Fasman, G. D.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 1975-06
Volume: 14
Issue: 11
Pages: 2536-2541
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi00682a037
OpenAlex: W1982005407
Cited by: 98
References: 0
Citations by year: 2026: 1 · 2025: 2 · 2024: 1 · 2019: 3 · 2014: 2 · 2013: 1
FWCI: 2.78
Type: journal article
Language: en
Open access: closed
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Keywords: glucagon, protein conformation, secondary structure prediction, alpha-helix, beta-sheet, beta-turn, circular dichroism, insulin, receptor binding, protein aggregation
MeSH terms: Amino Acid Sequence, Circular Dichroism, Glucagon, Mathematics, Protein Conformation, Structure-Activity Relationship

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Conformation of glucagon. Predictions and consequences

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