Possible biological roles for metastable proteins

Kenneth W. Nickerson, Richard A. Day

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

We feel it is important to point out certain complications stemming from some assumptions contained in current thinking on the relationship of protein conformation to primary sequence. 1) It is justifiably felt that the primary sequence of a protein determines its conformation in a given environment; this has been proven in many cases (Buckley, Whitney and Tanford, 1963; Deal, Rutter, Massey and Van Holde, 1963; Epstein, Goldberger and Afinsen, 1963). 2) It has become implicit in the thinking of many biochemists that the biologically active conformation of a protein is the most stable thermodynamically. We feel that it is a priori unlikely that these two assumptions are without important exceptions and would like to suggest a mechanistic approach for the additional proposal that some, proteins exist in their active form in a thermodynamically metastable state, and that this may have important biological implications.

Original languageEnglish (US)
Pages (from-to)303-306
Number of pages4
JournalBioSystems
Volume2
Issue number6
DOIs
StatePublished - Jun 1969

Fingerprint

Protein Conformation
Conformation
Proteins
Protein
Conformations
Metastable States
Complications
Exception

ASJC Scopus subject areas

  • Statistics and Probability
  • Modeling and Simulation
  • Biochemistry, Genetics and Molecular Biology(all)
  • Applied Mathematics

Cite this

Possible biological roles for metastable proteins. / Nickerson, Kenneth W.; Day, Richard A.

In: BioSystems, Vol. 2, No. 6, 06.1969, p. 303-306.

Research output: Contribution to journalArticle

Nickerson, Kenneth W. ; Day, Richard A. / Possible biological roles for metastable proteins. In: BioSystems. 1969 ; Vol. 2, No. 6. pp. 303-306.
@article{9c34019526e745a3a4359518429afd93,
title = "Possible biological roles for metastable proteins",
abstract = "We feel it is important to point out certain complications stemming from some assumptions contained in current thinking on the relationship of protein conformation to primary sequence. 1) It is justifiably felt that the primary sequence of a protein determines its conformation in a given environment; this has been proven in many cases (Buckley, Whitney and Tanford, 1963; Deal, Rutter, Massey and Van Holde, 1963; Epstein, Goldberger and Afinsen, 1963). 2) It has become implicit in the thinking of many biochemists that the biologically active conformation of a protein is the most stable thermodynamically. We feel that it is a priori unlikely that these two assumptions are without important exceptions and would like to suggest a mechanistic approach for the additional proposal that some, proteins exist in their active form in a thermodynamically metastable state, and that this may have important biological implications.",
author = "Nickerson, {Kenneth W.} and Day, {Richard A.}",
year = "1969",
month = "6",
doi = "10.1016/0303-2647(69)90016-1",
language = "English (US)",
volume = "2",
pages = "303--306",
journal = "BioSystems",
issn = "0303-2647",
publisher = "Elsevier Ireland Ltd",
number = "6",

}

TY - JOUR

T1 - Possible biological roles for metastable proteins

AU - Nickerson, Kenneth W.

AU - Day, Richard A.

PY - 1969/6

Y1 - 1969/6

N2 - We feel it is important to point out certain complications stemming from some assumptions contained in current thinking on the relationship of protein conformation to primary sequence. 1) It is justifiably felt that the primary sequence of a protein determines its conformation in a given environment; this has been proven in many cases (Buckley, Whitney and Tanford, 1963; Deal, Rutter, Massey and Van Holde, 1963; Epstein, Goldberger and Afinsen, 1963). 2) It has become implicit in the thinking of many biochemists that the biologically active conformation of a protein is the most stable thermodynamically. We feel that it is a priori unlikely that these two assumptions are without important exceptions and would like to suggest a mechanistic approach for the additional proposal that some, proteins exist in their active form in a thermodynamically metastable state, and that this may have important biological implications.

AB - We feel it is important to point out certain complications stemming from some assumptions contained in current thinking on the relationship of protein conformation to primary sequence. 1) It is justifiably felt that the primary sequence of a protein determines its conformation in a given environment; this has been proven in many cases (Buckley, Whitney and Tanford, 1963; Deal, Rutter, Massey and Van Holde, 1963; Epstein, Goldberger and Afinsen, 1963). 2) It has become implicit in the thinking of many biochemists that the biologically active conformation of a protein is the most stable thermodynamically. We feel that it is a priori unlikely that these two assumptions are without important exceptions and would like to suggest a mechanistic approach for the additional proposal that some, proteins exist in their active form in a thermodynamically metastable state, and that this may have important biological implications.

UR - http://www.scopus.com/inward/record.url?scp=0014530196&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014530196&partnerID=8YFLogxK

U2 - 10.1016/0303-2647(69)90016-1

DO - 10.1016/0303-2647(69)90016-1

M3 - Article

C2 - 5798530

AN - SCOPUS:0014530196

VL - 2

SP - 303

EP - 306

JO - BioSystems

JF - BioSystems

SN - 0303-2647

IS - 6

ER -