Evidence map›Paper›PMID 17765922›Full record

ArticleJournal of molecular biology2007

Increasing protein conformational stability by optimizing beta-turn sequence.

Saul R Trevino, Stephanie Schaefer, J Martin Scholtz, C Nick Pace

Abstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

60 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Saul R TrevinoDepartment of Molecular and Cellular Medicine, Texas A&M University System Health Science Center, College Station, TX 77843, USA.
Stephanie Schaefer
J Martin Scholtz
C Nick Pace

Funding

ENERGETICS AND MECHANISM OF FOLDING OF RIBONUCLEASE T1R01GM037039 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI PACE, CARLOS N · 1986 to 2006
$1.6M
LOCAL AND LONG RANGE INTERACTIONS IN PROTEIN FOLDINGR01GM052483 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI SCHOLTZ, J. MARTIN · 2001 to 2004
$806k
Graduate Training in Molecular BiophysicsT32GM065088 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI REINHART, GREGORY DUNCAN · 2003 to 2007
$572k
HIERARCHY OF PROTEIN FOLDING AND STABILITYR29GM052483 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI SCHOLTZ, J. MARTIN · 1995 to 1999
–
NIGMS NIH HHS GM 37039NIGMS NIH HHS GM 52483NIGMS NIH HHS R01 GM037039NIGMS NIH HHS R01 GM052483NIGMS NIH HHS R29 GM052483NIGMS NIH HHS T32 GM 065088NIGMS NIH HHS T32 GM065088
6 · The paper itself

Abstract

Protein conformational stability is an important concern in many fields. Here, we describe a strategy for significantly increasing conformational stability by optimizing beta-turn sequence. Proline and glycine residues are statistically preferred at several beta-turn positions, presumably because their unique side-chains contribute favorably to conformational stability in certain beta-turn positions. However, beta-turn sequences often deviate from preferred proline or preferred glycine. Therefore, our strategy involves replacing non-proline and non-glycine beta-turn residues with preferred proline or preferred glycine residues. Here, we develop guidelines for selecting appropriate mutations, and present results for five mutations (S31P, S42G, S48P, T76P, and Q77G) that significantly increase the conformational stability of RNase Sa. The increases in stability ranged from 0.7 kcal/mol to 1.3 kcal/mol. The strategy was successful in overlapping or isolated beta-turns, at buried (up to 50%) or completely exposed sites, and at relatively flexible or inflexible sites. Considering the significant number of beta-turn residues in every globular protein and the frequent deviation of beta-turn sequences from preferred proline and preferred glycine residues, this simple, efficient strategy will be useful for increasing the conformational stability of proteins.

Indexed as

Protein Structure, SecondaryGlycineModels, MolecularMutationProlineThermodynamicsGlycineProline

Identifiers

PMID17765922
PMCPMC2084202

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.